The health of dairy animals, particularly the milk-producing mammary glands, is essential to the dairy industry because of the crucial hygienic and economic aspects of ensuring production of high quality milk. Due to its high prevalence, mastitis is considered the most important threat to dairy industry, due to its impacts on animal health and milk production and thus on economic benefits. The MG is protected by several defence mechanisms that prevent microbial penetration and surveillance. However, several factors can attenuate the host immune response (IR), and the possession of various virulence and resistance factors by different mastitis-causing microorganisms greatly limits immune defences and promotes establishment of intramammary infections (IMIs). A comprehensive understanding of MG immunity in both healthy and inflammatory conditions will be an important key to understand the nature of IMIs caused by specific pathogens and greatly contributes to the development of effective control methods and appropriate detection techniques. Consequently, this review aims to provide a detailed overview of antimicrobial defences in the MG under healthy and inflammatory conditions. In this sense, we will focus on pathogen-dependent variations in IRs mounted by the host during IMI and discuss the potential ramifications of these variations. 1. Introduction The udder is the milk-producing organ of dairy animals; hence, for optimal production, it should be healthy. Mastitis is the inflammatory response of the mammary gland (MG) tissue to physiological and metabolic changes, traumas, and allergies and, most frequently, to injuries caused by various microorganisms. Mastitis is considered the utmost threat to the dairy industry from three perspectives: economic, hygienic, and legal (EU Directive 46/92, modified by Directive 71/94). The intramammary inflammation (IMI), accompanied by immunological and pathological changes in the MG tissue, occurs at different degrees of intensities and results in a wide range of consequences regarding physical, chemical, and often microbiological alterations of secreted milk. A wide spectrum of microorganisms, including fungi, yeast, algae, Chlamydia, and viruses, have been incriminated in causing mastitis, but bacteria remain the principle causative agents of such complex [1, 2]. The major bacterial mastitis pathogens (Staphylococcus aureus, Streptococcus agalactiae, S. uberis, S. dysgalactiae, and coliforms) are most often responsible for clinical mastitis (CM). Meanwhile, minor pathogens (coagulase-negative staphylococci “CNS”;
References
[1]
R. J. Harmon, “Physiology of mastitis and factors affecting somatic cell counts,” Journal of Dairy Science, vol. 77, no. 7, pp. 2103–2112, 1994.
[2]
N. Sudhan and N. Sharma, “Mastitis- an important production disease of dairy animals,” in Gurgoan: Sarva Manav Vikash Samiti, pp. 72–88, 2010.
[3]
A. Zecconi, J. Hamanno, V. Bronzo, P. Moroni, G. Giovannini, and R. Piccinini, “Relationship between teat tissue immune defences and intramammary infections,” in Biology of the Mammary Gland, pp. 287–293, Springer, New York, NY, USA, 2002.
[4]
L. M. Sordillo and K. L. Streicher, “Mammary gland immunity and mastitis susceptibility,” Journal of Mammary Gland Biology and Neoplasia, vol. 7, no. 2, pp. 135–146, 2002.
[5]
L. M. Sordillo, K. Shafer-Weaver, and D. DeRosa, “Immunobiology of the mammary gland,” Journal of Dairy Science, vol. 80, no. 8, pp. 1851–1865, 1997.
[6]
K. P. Waller, “Mammary gland immunology around parturition,” in Biology of the Mammary Gland, pp. 231–245, Springer, New York, NY, USA, 2002.
[7]
L. M. Sordillo, “Factors affecting mammary gland immunity and mastitis susceptibility,” Livestock Production Science, vol. 98, no. 1-2, pp. 89–99, 2005.
[8]
S. C. Nickerson, “Immune mechanisms of the bovine udder: an overview,” Journal of the American Veterinary Medical Association, vol. 187, no. 1, pp. 41–45, 1985.
[9]
C. O. Paulrud, “Basic concepts of the bovine teat canal,” Veterinary Research Communications, vol. 29, no. 3, pp. 215–245, 2005.
[10]
K. G. Hibbitt and M. Benians, “Some effects in vivo of the teat canal and effects in vitro of cationic proteins on Staphylococci.,” Journal of General Microbiology, vol. 68, no. 1, pp. 123–128, 1971.
[11]
R. Gennaro, B. Dewald, U. Horisberger, H. U. Gubler, and M. Baggiolini, “A novel type of cytoplasmic granule in bovine neutrophils,” Journal of Cell Biology, vol. 96, no. 6, pp. 1651–1661, 1983.
[12]
J. Bitman, D. L. Wood, S. A. Bright et al., “Lipid composition of teat canal keratin collected before and after milking from Holstein and Jersey cows,” Journal of Dairy Science, vol. 74, no. 2, pp. 414–420, 1991.
[13]
J. Bitman, D. L. Wood, S. A. Bright, and R. H. Miller, “Lipid composition of bovine teat canal keratin,” Journal of Dairy Science, vol. 71, no. 5, pp. 1389–1395, 1988.
[14]
R. H. Miller, J. Bitman, S. A. Bright, D. L. Wood, and A. V. Capuco, “Effect of clinical and subclinical mastitis on lipid composition of teat canal keratin,” Journal of Dairy Science, vol. 75, no. 6, pp. 1436–1442, 1992.
[15]
D. Wood, S. Bright, A. Capuco, P. Grier, R. Miller, and J. Bitman, “The effect of clinical mastitis on lipid composition of teat canal keratin and milk,” Journal of Dairy Science, vol. 73, supplement 1, p. 213, 1990.
[16]
M. Rinaldi, R. W. Li, D. D. Bannerman, et al., “A sentinel function for teat tissues in dairy cows: dominant innate immune response elements define early response to E. coli mastitis,” Functional & Integrative Genomics, vol. 10, no. 1, pp. 21–38, 2010.
[17]
C. J. Whelehan, K. G. Meade, P. D. Eckersall, F. J. Young, and C. O'Farrelly, “Experimental Staphylococcus aureus infection of the mammary gland induces region-specific changes in innate immune gene expression,” Veterinary Immunology and Immunopathology, vol. 140, no. 3-4, pp. 181–189, 2011.
[18]
S. C. Nickerson, “Resistance mechanisms of the bovine udder: New implications for mastitis control at the teat end,” Journal of the American Veterinary Medical Association, vol. 191, no. 11, pp. 1484–1488, 1987.
[19]
A. V. Capuco, G. A. Mein, S. C. Nickerson et al., “Influence of pulsationless milking on teat canal keratin and mastitis,” Journal of Dairy Science, vol. 77, no. 1, pp. 64–74, 1994.
[20]
A. J. Bramley and F. H. Dodd, “Reviews of the progress of dairy science: mastitis control-progress and prospects,” Journal of Dairy Research, vol. 51, no. 3, pp. 481–512, 1984.
[21]
A. V. Capuco, S. A. Bright, J. W. Pankey, D. L. Wood, R. H. Miller, and J. Bitman, “Increased susceptibility to intramammary infection following removal of teat canal keratin,” Journal of dairy science, vol. 75, no. 8, pp. 2126–2130, 1992.
[22]
N. Craven and M. R. Williams, “Defences of the bovine mammary gland against infection and prospects for their enhancement,” Veterinary Immunology and Immunopathology, vol. 10, no. 1, pp. 71–127, 1985.
[23]
D. Williams and G. Mein, “The role of machine milking in the invasion of mastitis organisms and implications for maintaining low infection rates,” Kieler Milchwirtschaftliche Forschungsberichte, vol. 37, pp. 415–425, 1985.
[24]
F. H. S. Newbould and F. K. Neave, “The effect of inoculating the bovine teat duct with small numbers of Staphylococcus aureus,” Journal of Dairy Research, vol. 32, no. 2, pp. 171–179, 1965.
[25]
P. Rainard and C. Riollet, “Innate immunity of the bovine mammary gland,” Veterinary Research, vol. 37, no. 3, pp. 369–400, 2006.
[26]
T. K. Griffin, R. L. Williams, R. J. Grindal, F. K. Neave, and D. R. Westgarth, “Use of deflector shields to reduce intramammary infection by preventing impacts on the teat ends of cows during machine milking,” Journal of Dairy Research, vol. 50, no. 4, pp. 397–404, 1983.
[27]
C. Riollet, P. Rainard, and B. Poutrel, “Cells and cytokines in inflammatory secretions of bovine mammary gland,” Advances in Experimental Medicine and Biology, vol. 480, pp. 247–258, 2000.
[28]
B. C. Taylor, J. D. Dellinger, J. S. Cullor, and J. L. Stott, “Bovine milk lymphocytes display the phenotype of memory T cells and are predominantly CD8+,” Cellular Immunology, vol. 156, no. 1, pp. 245–253, 1994.
[29]
P. M. Outteridge and C. S. Lee, “Cellular immunity in the mammary gland with particular reference to T, B lymphocytes and macrophages,” Advances in Experimental Medicine and Biology, vol. 137, pp. 513–534, 1981.
[30]
I. Roitt, J. Brostoff, and D. Male, Immunology, Mosby, Philadelphia, Pa, USA, 2001.
[31]
C. Concha, O. Holmberg, and B. Morein, “Characterization and response to mitogens of mammary lymphocytes from the bovine dry-period secretion,” Journal of Dairy Research, vol. 47, no. 3, pp. 305–311, 1980.
[32]
C. Concha, O. Holmberg, and B. Morein, “Proportion of B- and T-lymphocytes in normal bovine milk,” Journal of Dairy Research, vol. 45, no. 2, pp. 287–290, 1978.
[33]
K. Stelwagen, E. Carpenter, B. Haigh, A. Hodgkinson, and T. T. Wheeler, “Immune components of bovine colostrum and milk,” Journal of Animal Science, vol. 87, no. 13, pp. 3–9, 2009.
[34]
S. Uthaisangsook, N. K. Day, S. L. Bahna, R. A. Good, and S. Haraguchi, “Innate immunity and its role against infections,” Annals of Allergy, Asthma and Immunology, vol. 88, no. 3, pp. 253–264, 2002.
[35]
S. Akira and K. Takeda, “Toll-like receptor signalling,” Nature Reviews Immunology, vol. 4, no. 7, pp. 499–511, 2004.
[36]
S. Akira, S. Uematsu, and O. Takeuchi, “Pathogen recognition and innate immunity,” Cell, vol. 124, no. 4, pp. 783–801, 2006.
[37]
D. D. Bannerman, A. Chockalingam, M. J. Paape, and J. C. Hope, “The bovine innate immune response during experimentally-induced Pseudomonas aeruginosa mastitis,” Veterinary Immunology and Immunopathology, vol. 107, no. 3-4, pp. 201–215, 2005.
[38]
C. Gray, Y. Strandberg, L. Donaldson, and R. L. Tellam, “Bovine mammary epithelial cells, initiators of innate immune responses to mastitis,” Australian Journal of Experimental Agriculture, vol. 45, no. 7-8, pp. 757–761, 2005.
[39]
M. R. Barber, A. G. Pantschenko, L. S. Hinckley, and T. J. Yang, “Inducible and constitutive in vitro neutrophil chemokine expression by mammary epithelial and myoepithelial cells,” Clinical and Diagnostic Laboratory Immunology, vol. 6, no. 6, pp. 791–798, 1999.
[40]
K. Singh, S. R. Davis, J. M. Dobson et al., “cDNA microarray analysis reveals that antioxidant and immune genes are upregulated during involution of the bovine mammary gland,” Journal of Dairy Science, vol. 91, no. 6, pp. 2236–2246, 2008.
[41]
M. E. Kehrli Jr. and D. E. Shuster, “Factors affecting milk somatic cells and their role in health of the bovine mammary gland,” Journal of Dairy Science, vol. 77, no. 2, pp. 619–627, 1994.
[42]
D. J. Hurley, M. H. Kensinger, A. M. Mastro, and R. A. Wilson, “An evaluation of the mononuclear cells eerived from bovine mammary gland dry secretions using leukocyte antigen specific monoclonal antibodies, light scattering properties and non-specific esterase staining,” Veterinary Immunology and Immunopathology, vol. 25, no. 2, pp. 177–193, 1990.
[43]
C. S. Lee, F. B. Wooding, and P. Kemp, “Identification, properties, and differential counts of cell populations using electron microscopy of dry cows secretions, colostrum and milk from normal cows,” Journal of Dairy Research, vol. 47, no. 1, pp. 39–50, 1980.
[44]
L. Weber, E. Peterhans, and R. Wyler, “The chemiluminescent response of bovine polymorphonuclear leucocytes isolated from milk and blood,” Veterinary Immunology and Immunopathology, vol. 4, no. 3, pp. 397–412, 1983.
[45]
A. Bradley and M. Green, “Use and interpretation of somatic cell count data in dairy cows,” In Practice, vol. 27, no. 6, pp. 310–315, 2005.
[46]
M. J. Paape and A. J. Guidry, “Effect of milking on leucocytes in the subcutaneous abdominal vein of the cow,” Journal of Dairy Science, vol. 52, no. 7, pp. 998–1002, 1969.
[47]
Y. Lin, L. Xia, J. D. Turner, and X. Zhao, “Morphologic observation of neutrophil diapedesis across bovine mammary gland epithelium in vitro,” The American Journal of Veterinary Research, vol. 56, no. 2, pp. 203–207, 1995.
[48]
R. M. Akers and S. C. Nickerson, “Mastitis and its impact on structure and function in the ruminant mammary gland,” Journal of Mammary Gland Biology and Neoplasia, vol. 16, no. 4, pp. 275–289, 2011.
[49]
M. J. Paape, K. Shafer-Weaver, A. V. Capuco, K. Van Oostveldt, and C. Burvenich, “Immune surveillance of mammary tissue by phagocytic cells,” Advances in Experimental Medicine and Biology, vol. 480, pp. 259–277, 2000.
[50]
H. Dosogne, C. Burvenich, T. Van Werven, E. Roets, E. N. Noordhuizen-Stassen, and B. Goddeeris, “Increased surface expression of CD11b receptors on polymorphonuclear leukocytes is not sufficient to sustain phagocytosis during Escherichia coli mastitis in early postpartum dairy cows,” Veterinary Immunology and Immunopathology, vol. 60, no. 1-2, pp. 47–59, 1997.
[51]
M. R. Barber and T. J. Yang, “Chemotactic activities in nonmastitic and mastitic mammary secretions: presence of interleukin-8 in mastitic but not nonmastitic secretions,” Clinical and Diagnostic Laboratory Immunology, vol. 5, no. 1, pp. 82–86, 1998.
[52]
A. DiCarlo and M. Paape, “Comparison of C3b binding to bovine peripheral blood and mammary gland neutrophils (PMN),” American Journal of Veterinary Research, vol. 57, pp. 151–156, 1996.
[53]
M. B. Barrio, P. Rainard, and B. Poutrel, “Milk complement and the opsonophagocytosis and killing of Staphylococcus aureus mastitis isolates by bovine neutrophils,” Microbial Pathogenesis, vol. 34, no. 1, pp. 1–9, 2003.
[54]
M. Paape, E. Lilius, P. Wiitanen, M. Kontio, and R. Miller, “Intramammary defense against infections induced by Escherichia coli in cows,” American Journal of Veterinary Research, vol. 57, no. 4, pp. 477–482, 1996.
[55]
A. Matsukawa, “Neutrophils as a source of cytokines in inflammation,” Histology and Histopathology, vol. 14, no. 2, pp. 511–516, 1999.
[56]
U. Bank and S. Ansorge, “More than destructive: neutrophil-derived serine proteases in cytokine bioactivity control,” Journal of Leukocyte Biology, vol. 69, no. 2, pp. 197–206, 2001.
[57]
M. E. Selsted, Y. Q. Tang, W. L. Morris et al., “Purification, primary structures, and antibacterial activities of β-defensins, a new family of antimicrobial peptides from bovine neutrophils,” Journal of Biological Chemistry, vol. 268, no. 9, pp. 6641–6648, 1993.
[58]
A. Linde, C. R. Ross, E. G. Davis, L. Dib, F. Blecha, and T. Melgarejo, “Innate immunity and host defense peptides in veterinary medicine,” Journal of Veterinary Internal Medicine, vol. 22, no. 2, pp. 247–265, 2008.
[59]
F. Moussaoui, F. Vangroenweghe, K. Haddadi et al., “Proteolysis in milk during experimental Escherichia coli mastitis,” Journal of Dairy Science, vol. 87, no. 9, pp. 2923–2931, 2004.
[60]
F. Moussaoui, I. Michelutti, Y. Le Roux, and F. Laurent, “Mechanisms involved in milk endogenous proteolysis induced by a lipopolysaccharide experimental mastitis,” Journal of Dairy Science, vol. 85, no. 10, pp. 2562–2570, 2002.
[61]
J. P. Opdebeeck, “Mammary gland immunity,” Journal of the American Veterinary Medical Association, vol. 181, no. 10, pp. 1061–1065, 1982.
[62]
C. Prin-Mathieu, Y. Le Roux, G. C. Faure, F. Laurent, M. C. Béné, and F. Moussaoui, “Enzymatic activities of bovine peripheral blood leukocytes and milk polymorphonuclear neutrophils during intramammary inflammation caused by lipopolysaccharide,” Clinical and Diagnostic Laboratory Immunology, vol. 9, no. 4, pp. 812–817, 2002.
[63]
M. J. Paape, D. D. Bannerman, X. Zhao, and J.-W. Lee, “The bovine neutrophil: structure and function in blood and milk,” Veterinary Research, vol. 34, no. 5, pp. 597–627, 2003.
[64]
M. Paape, J. Mehrzad, X. Zhao, J. Detilleux, and C. Burvenich, “Defense of the bovine mammary gland by polymorphonuclear neutrophil leukocytes,” Journal of Mammary Gland Biology and Neoplasia, vol. 7, no. 2, pp. 109–121, 2002.
[65]
J. Ten Napel, Y. de Haas, G. de Jong, T. J. G. M. Lam, W. Ouweltjes, and J. J. Windig, “Characterization of distributions of somatic cell counts,” Journal of Dairy Science, vol. 92, no. 3, pp. 1253–1264, 2009.
[66]
D. L. Jensen and R. J. Eberhart, “Total and differential cell counts in secretions of the nonlactating bovine mammary gland,” The American Journal of Veterinary Research, vol. 42, no. 5, pp. 743–747, 1981.
[67]
N. Craven, “Generation of neutrophil chemoattractants by phagocytosing bovine mammary macrophages,” Research in Veterinary Science, vol. 35, no. 3, pp. 310–317, 1983.
[68]
I. Politis, X. Zhao, B. W. McBride, and J. H. Burton, “Function of bovine mammary macrophages as antigen-presenting cells,” Veterinary Immunology and Immunopathology, vol. 30, no. 4, pp. 399–410, 1992.
[69]
J. L. Fitzpatrick, P. J. Cripps, A. W. Hill, P. W. Bland, and C. R. Stokes, “MHC class II expression in the bovine mammary gland,” Veterinary Immunology and Immunopathology, vol. 32, no. 1-2, pp. 13–23, 1992.
[70]
M. Denis, N. A. Parlane, S. J. Lacy-Hulbert, E. L. Summers, B. M. Buddle, and D. N. Wedlock, “Bactericidal activity of macrophages against Streptococcus uberis is different in mammary gland secretions of lactating and drying off cows,” Veterinary Immunology and Immunopathology, vol. 114, no. 1-2, pp. 111–120, 2006.
[71]
N. A. Mullan, E. A. Carter, and K. A. Nguyen, “Phagocytic and bactericidal properties of bovine macrophages from non-lactating mammary glands,” Research in Veterinary Science, vol. 38, no. 2, pp. 160–166, 1985.
[72]
R. H. Miller, A. J. Guidry, M. J. Paape, A. M. Dulin, and L. A. Fulton, “Relationship between immunoglobulin concentrations in milk and phagocytosis by bovine neutrophils,” American Journal of Veterinary Research, vol. 49, no. 1, pp. 42–45, 1988.
[73]
C. R. Rossi and G. K. Kiesel, “Bovine immunoglobulin G subclass receptor sites on bovine macrophages,” The American Journal of Veterinary Research, vol. 38, no. 7, pp. 1023–1025, 1977.
[74]
M. Caroprese, A. Marzano, L. Schena, R. Marino, A. Santillo, and M. Albenzio, “Contribution of macrophages to proteolysis and plasmin activity in ewe bulk milk,” Journal of Dairy Science, vol. 90, no. 6, pp. 2767–2772, 2007.
[75]
K. Persson, I. Larsson, and C. H. Sandgren, “Effects of certain inflammatory mediators on bovine neutrophil migration in vivo and in vitro,” Veterinary Immunology and Immunopathology, vol. 37, no. 2, pp. 99–112, 1993.
[76]
K. A. Shafer-Weaver and L. M. Sordillo, “Bovine CD8+ suppressor lymphocytes alter immune responsiveness during the postpartum period,” Veterinary Immunology and Immunopathology, vol. 56, no. 1-2, pp. 53–64, 1997.
[77]
K. A. Shafer-Weaver, G. M. Pighetti, and L. M. Sordillo, “Diminished mammary gland lymphocyte functions parallel shifts in trafficking patterns during the postpartum period,” Experimental Biology and Medicine, vol. 212, no. 3, pp. 271–279, 1996.
[78]
Y. H. Park, L. K. Fox, M. J. Hamilton, and W. C. Davis, “Suppression of proliferative response of BoCD4+ T lymphocytes by activated BoCD8+ T lymphocytes in the mammary gland of cows with Staphylococcus aureus mastitis,” Veterinary Immunology and Immunopathology, vol. 36, no. 2, pp. 137–151, 1993.
[79]
T. Hisatsune, A. Enomoto, K.-I. Nishijima et al., “CD8+ suppressor T cell clone capable of inhibiting the antigen- and anti-T cell receptor-induced proliferation of Th clones without cytolytic activity,” Journal of Immunology, vol. 145, no. 8, pp. 2421–2426, 1990.
[80]
Y. H. Park, L. K. Fox, M. J. Hamilton, and W. C. Davis, “Bovine mononuclear leukocyte subpopulations in peripheral blood and mammary gland secretions during lactation,” Journal of dairy science, vol. 75, no. 4, pp. 998–1006, 1992.
[81]
M. Worku, M. J. Paape, and W. W. Marquardt, “Modulation of Fc receptors for IgG on bovine polymorphonuclear neutrophils by interferon-γ through de novo RNA transcription and protein synthesis,” The American Journal of Veterinary Research, vol. 55, no. 2, pp. 234–238, 1994.
[82]
N. D. Machugh, J. K. Mburu, M. J. Carol, C. R. Wyatt, J. A. Orden, and W. C. Davis, “Identification of two distinct subsets of bovine γδ T cells with unique cell surface phenotype and tissue distribution,” Immunology, vol. 92, no. 3, pp. 340–345, 1997.
[83]
C. R. Mackay and W. R. Hein, “Marked variations in γδ T cell numbers and distribution throughout the life of sheep,” Current Topics in Microbiology and Immunology, vol. 173, pp. 107–111, 1991.
[84]
C. R. Mackay, W. R. Hein, M. H. Brown, and P. Matzinger, “Unusual expression of CD2 in sheep: implications for T cell interactions,” European Journal of Immunology, vol. 18, no. 11, pp. 1681–1688, 1988.
[85]
J. P. Allison and W. L. Havran, “The immunobiology of T cells with invariant γδ antigen receptors,” Annual Review of Immunology, vol. 9, no. 1, pp. 679–705, 1991.
[86]
C. Riollet, P. Rainard, and B. Poutrel, “Cell subpopulations and cytokine expression in cow milk in response to chronic Staphylococcus aureus infection,” Journal of Dairy Science, vol. 84, no. 5, pp. 1077–1084, 2001.
[87]
B. A. Mallard, J. C. Dekkers, M. J. Ireland et al., “Alteration in immune responsiveness during the peripartum period and its ramification on dairy cow and calf health,” Journal of Dairy Science, vol. 81, no. 2, pp. 585–595, 1998.
[88]
A. Hoek, V. P. M. G. Rutten, J. Kool et al., “Subpopulations of bovine WC1+ T cells rather than CD4+CD25highFoxp3+ T cells act as immune regulatory cells ex vivo,” Veterinary Research, vol. 40, no. 1, p. 6, 2009.
[89]
G. Trinchieri, “Biology of natural killer cells,” Advances in Immunology, vol. 47, pp. 187–376, 1989.
[90]
E. Vivier, D. H. Raulet, A. Moretta et al., “Innate or adaptive immunity? The example of natural killer cells,” Science, vol. 331, no. 6013, pp. 44–49, 2011.
[91]
K. A. Shafer-Weaver and L. M. Sordillo, “Enhancing bactericidal activity of bovine lymphoid cells during the periparturient period,” Journal of Dairy Science, vol. 79, no. 8, pp. 1347–1352, 1996.
[92]
L. M. Sordillo, J. T. Kendall, C. M. Corl, and T. H. Cross, “Molecular characterization of a saposin-like protein family member isolated from bovine lymphocytes,” Journal of Dairy Science, vol. 88, no. 4, pp. 1378–1390, 2005.
[93]
R. Miller, M. Paape, L. Fulton, and M. Schutz, “The relationship of milk somatic cell count to milk yields for Holstein heifers after first calving,” Journal of Dairy Science, vol. 76, no. 3, pp. 728–733, 1993.
[94]
J. S. McDonald and A. J. Anderson, “Total and differential somatic cell counts in secretions from noninfected bovine mammary glands: the early nonlactating period,” American Journal of Veterinary Research, vol. 42, no. 8, pp. 1360–1365, 1981.
[95]
A. Pengov, “The role of coagulase-negative Staphylococcus spp. and associated somatic cell counts in the ovine mammary gland,” Journal of Dairy Science, vol. 84, no. 3, pp. 572–574, 2001.
[96]
C. Cuccuru, P. Moroni, A. Zecconi, S. Casu, A. Caria, and A. Contini, “Milk differential cell counts in relation to total counts in Sardinian ewes,” Small Ruminant Research, vol. 25, no. 2, pp. 169–173, 1997.
[97]
M. Morgante, S. Ranucci, M. Pauselli, C. Casoli, and E. Duranti, “Total and differential cell count in milk of primiparous Comisana ewes without clinical signs of mastitis,” Small Ruminant Research, vol. 21, no. 3, pp. 265–271, 1996.
[98]
M. J. Paape, G. R. Wiggans, D. D. Bannerman et al., “Monitoring goat and sheep milk somatic cell counts,” Small Ruminant Research, vol. 68, no. 1-2, pp. 114–125, 2007.
[99]
M. Albenzio, A. Santillo, M. Caroprese, D. Ruggieri, M. Ciliberti, and A. Sevi, “Immune competence of the mammary gland as affected by somatic cell and pathogenic bacteria in ewes with subclinical mastitis,” Journal of Dairy Science, vol. 95, no. 7, pp. 3877–3887, 2012.
[100]
A. M. Dulin, M. J. Paape, W. D. Schultze, and B. T. Weinland, “Effect of parity, stage of lactation, and intramammary infection on concentration of somatic cells and cytoplasmic particles in goat milk,” Journal of dairy science, vol. 66, no. 11, pp. 2426–2433, 1983.
[101]
A. Dulin, M. Paape, and W. Wergin, “Differentiation and enumeration of somatic cells in goat milk,” Journal of Food Protection, vol. 45, no. 5, pp. 435–439, 1982.
[102]
N. Manlongat, T. J. Yang, L. S. Hinckley, R. B. Bendel, and H. M. Krider, “Physiologic-chemoattractant-induced migration of polymorphonuclear leukocytes in milk,” Clinical and Diagnostic Laboratory Immunology, vol. 5, no. 3, pp. 375–381, 1998.
[103]
E. A. Droke, M. J. Paape, and A. L. di Carlo, “Prevalence of high somatic cell counts in bulk tank goat milk,” Journal of Dairy Science, vol. 76, no. 4, pp. 1035–1039, 1993.
[104]
G. F. W. Haenlein, “Relationship of somatic cell counts in goat milk to mastitis and productivity,” Small Ruminant Research, vol. 45, no. 2, pp. 163–178, 2002.
[105]
A. Contreras, “Mamitis caprina II,” Ovis, vol. 54, p. 114, 1998.
[106]
M. Paape, B. Poutrel, A. Contreras, J. C. Marco, and A. Capuco, “Milk somatic cells and lactation in small ruminants,” Journal of Dairy Science, vol. 84, pp. E237–E244, 2001.
[107]
A. M. Rota, C. Gonzalo, P. L. Rodriguez, A. I. Rojas, L. Martin, and J. J. Tovar, “Somatic cell types in goats milk in relation to total cell count, stage and number of lactation,” Small Ruminant Research, vol. 12, no. 1, pp. 89–98, 1993.
[108]
M. F. Addis, S. Pisanu, G. Marogna et al., “Production and release of antimicrobial and immune defense proteins by mammary epithelial cells following Streptococcus uberis infection of sheep,” Infection and Immunity, vol. 81, no. 9, pp. 3182–3197, 2013.
[109]
A. Porcherie, P. Cunha, A. Trotereau et al., “Repertoire of Escherichia coli agonists sensed by innate immunity receptors of the bovine udder and mammary epithelial cells,” Veterinary Research, vol. 43, article 14, 2012.
[110]
G. M. Barrington, T. B. McFadden, M. T. Huyler, and T. E. Besser, “Regulation of colostrogenesis in cattle,” Livestock Production Science, vol. 70, no. 1-2, pp. 95–104, 2001.
[111]
O. Wellnitz and D. E. Kerr, “Cryopreserved bovine mammary cells to model epithelial response to infection,” Veterinary Immunology and Immunopathology, vol. 101, no. 3-4, pp. 191–202, 2004.
[112]
N. Boudjellab, H. S. Chan-Tang, X. Li, and X. Zhao, “Interleukin 8 response by bovine mammary epithelial cells to lipopolysaccharide stimulation,” The American Journal of Veterinary Research, vol. 59, no. 12, pp. 1563–1567, 1998.
[113]
C. A. Michie, E. Tantscher, T. Schall, and A. Rot, “Physiological secretion of chemokines in human breast milk,” European Cytokine Network, vol. 9, no. 2, pp. 123–129, 1998.
[114]
H. Lahouassa, E. Moussay, P. Rainard, and C. Riollet, “Differential cytokine and chemokine responses of bovine mammary epithelial cells to Staphylococcus aureus and Escherichia coli,” Cytokine, vol. 38, no. 1, pp. 12–21, 2007.
[115]
R. L. Chandler, K. Smith, and B. A. Turfrey, “Studies on the phagocytic potential of secretory epithelial cells in experimental mastitis,” Journal of Comparative Pathology, vol. 90, no. 3, pp. 385–394, 1980.
[116]
L. Sanchez, L. Lujan, R. Oria et al., “Synthesis of lactoferrin and transport of transferrin in the lactating mammary gland of sheep,” Journal of Dairy Science, vol. 75, no. 5, pp. 1257–1262, 1992.
[117]
K. Swanson, S. Gorodetsky, L. Good et al., “Expression of a β-defensin mRNA, lingual antimicrobial peptide, in bovine mammary epithelial tissue is induced by mastitis,” Infection and Immunity, vol. 72, no. 12, pp. 7311–7314, 2004.
[118]
N. Isobe, J. Nakamura, H. Nakano, and Y. Yoshimura, “Existence of functional lingual antimicrobial peptide in bovine milk,” Journal of Dairy Science, vol. 92, no. 6, pp. 2691–2695, 2009.
[119]
N. W. J. Schr？der, S. Morath, C. Alexander et al., “Lipoteichoic acid (LTA) of Streptococcus pneumoniae and Staphylococcus aureus activates immune cells via Toll-like receptor (TLR)-2, lipopolysaccharide-binding protein (LBP), and CD14, whereas TLR-4 and MD-2 are not involved,” The Journal of Biological Chemistry, vol. 278, no. 18, pp. 15587–15594, 2003.
[120]
D. C. Fitzgerald, K. G. Meade, A. N. McEvoy et al., “Tumour necrosis factor-α (TNF-α) increases nuclear factor κB (NFκB) activity in and interleukin-8 (IL-8) release from bovine mammary epithelial cells,” Veterinary Immunology and Immunopathology, vol. 116, no. 1-2, pp. 59–68, 2007.
[121]
C. Riollet, D. Mutuel, M. Duonor-Cérutti, and P. Rainard, “Determination and characterization of bovine interleukin-17 cDNA,” Journal of Interferon and Cytokine Research, vol. 26, no. 3, pp. 141–149, 2006.
[122]
B. E. Brooker, “Pseudopod formation and phagocytosis of milk components by epithelial cells of the bovine mammary gland,” Cell and Tissue Research, vol. 229, no. 3, pp. 639–650, 1983.
[123]
R. C. Sprong, M. F. E. Hulstein, and R. van der Meer, “Bactericidal activities of milk lipids,” Antimicrobial Agents and Chemotherapy, vol. 45, no. 4, pp. 1298–1301, 2001.
[124]
J. T. Hancock, V. Salisbury, M. C. Ovejero-Boglione et al., “Antimicrobial properties of milk: dependence on presence of xanthine oxidase and nitrite,” Antimicrobial Agents and Chemotherapy, vol. 46, no. 10, pp. 3308–3310, 2002.
[125]
Y. Strandberg, C. Gray, T. Vuocolo, L. Donaldson, M. Broadway, and R. Tellam, “Lipopolysaccharide and lipoteichoic acid induce different innate immune responses in bovine mammary epithelial cells,” Cytokine, vol. 31, no. 1, pp. 72–86, 2005.
[126]
O. Wellnitz and R. M. Bruckmaier, “The innate immune response of the bovine mammary gland to bacterial infection,” Veterinary Journal, vol. 192, no. 2, pp. 148–152, 2012.
[127]
D. E. Shuster, E. K. Lee, and M. E. Kehrli Jr., “Bacterial growth, inflammatory cytokine production, and neutrophil recruitment during coliform mastitis in cows within ten days after calving, compared with cows at midlactation,” The American Journal of Veterinary Research, vol. 57, no. 11, pp. 1569–1575, 1996.
[128]
H. D. Brightbill and R. L. Modlin, “Toll-like receptors: molecular mechanisms of the mammalian immune response,” Immunology, vol. 101, no. 1, pp. 1–10, 2000.
[129]
S. Elazar, E. Gonen, A. Livneh-Kol, I. Rosenshine, and N. Y. Shpigel, “Neutrophil recruitment in endotoxin-induced murine mastitis is strictly dependent on mammary alveolar macrophages,” Veterinary Research, vol. 41, no. 1, pp. 1–14, 2010.
[130]
S. Mitterhuemer, W. Petzl, S. Krebs et al., “Escherichia coli infection induces distinct local and systemic transcriptome responses in the mammary gland,” BMC Genomics, vol. 11, no. 1, article 138, 2010.
[131]
W. Petzl, H. Zerbe, J. Günther et al., “Escherichia coli, but not Staphylococcus aureus triggers an early increased expression of factors contributing to the innate immune defense in the udder of the cow,” Veterinary Research, vol. 39, no. 2, pp. 1–23, 2008.
[132]
T. Goldammer, H. Zerbe, A. Molenaar et al., “Mastitis increases mammary mRNA abundance of β-defensin 5, toll-like-receptor 2 (TLR2), and TLR4 but not TLR9 in cattle,” Clinical and Diagnostic Laboratory Immunology, vol. 11, no. 1, pp. 174–185, 2004.
[133]
J. Günther, D. Koczan, W. Yang et al., “Assessment of the immune capacity of mammary epithelial cells: comparison with mammary tissue after challenge with Escherichia coli,” Veterinary Research, vol. 40, no. 4, pp. 1–14, 2009.
[134]
B. Griesbeck-Zilch, H. H. D. Meyer, C. Kühn, M. Schwerin, and O. Wellnitz, “Staphylococcus aureus and Escherichia coli cause deviating expression profiles of cytokines and lactoferrin messenger ribonucleic acid in mammary epithelial cells,” Journal of Dairy Science, vol. 91, no. 6, pp. 2215–2224, 2008.
[135]
W. Yang, H. Zerbe, W. Petzl et al., “Bovine TLR2 and TLR4 properly transduce signals from Staphylococcus aureus and E. coli, but S. aureus fails to both activate NF-κB in mammary epithelial cells and to quickly induce TNFα and interleukin-8 (CXCL8) expression in the udder,” Molecular Immunology, vol. 45, no. 5, pp. 1385–1397, 2008.
[136]
M. Menzies and A. Ingham, “Identification and expression of Toll-like receptors 1-10 in selected bovine and ovine tissues,” Veterinary Immunology and Immunopathology, vol. 109, no. 1-2, pp. 23–30, 2006.
[137]
R. Medzhitov, “Toll-like receptors and innate immunity,” Nature Reviews Immunology, vol. 1, no. 2, pp. 135–145, 2001.
[138]
O. Takeuchi, T. Kawai, P. F. Mühlradt et al., “Discrimination of bacterial lipoproteins by Toll-like recepttor 6,” International Immunology, vol. 13, no. 7, pp. 933–940, 2001.
[139]
O. Takeuchi, S. Sato, T. Horiuchi et al., “Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins,” Journal of Immunology, vol. 169, no. 1, pp. 10–14, 2002.
[140]
H. Kumar, T. Kawai, and S. Akira, “Pathogen recognition by the innate immune system,” International Reviews of Immunology, vol. 30, no. 1, pp. 16–34, 2011.
[141]
J. M. Devaney, C. M. Greene, C. C. Taggart, T. P. Carroll, S. J. O'Neill, and N. G. McElvaney, “Neutrophil elastase up-regulates interleukin-8 via toll-like receptor 4,” FEBS Letters, vol. 544, no. 1–3, pp. 129–132, 2003.
[142]
S. Epelman, D. Stack, C. Bell et al., “Different domains of Pseudomonas aeruginosa exoenzyme S activate distinct TLRs,” Journal of Immunology, vol. 173, no. 3, pp. 2031–2040, 2004.
[143]
E. J. Sohn, M. J. Paape, D. D. Bannerman, E. E. Connor, R. H. Fetterer, and R. R. Peters, “Shedding of sCD14 by bovine neutrophils following activation with bacterial lipopolysaccharide results in down-regulation of IL-8,” Veterinary Research, vol. 38, no. 1, pp. 95–108, 2007.
[144]
S. Bougarn, P. Cunha, A. Harmache, A. Fromageau, F. B. Gilbert, and P. Rainard, “Muramyl dipeptide synergizes with Staphylococcus aureus lipoteichoic acid to recruit neutrophils in the mammary gland and to stimulate mammary epithelial cells,” Clinical and Vaccine Immunology, vol. 17, no. 11, pp. 1797–1809, 2010.
[145]
S. R. Vavricka, M. W. Musch, J. E. Chang et al., “hPepT1 transports muramyl dipeptide, activating NF-κB and stimulating IL-8 secretion in human colonic Caco2/bbe cells,” Gastroenterology, vol. 127, no. 5, pp. 1401–1409, 2004.
[146]
S. Pandey and D. K. Agrawal, “Immunobiology of Toll-like receptors: emerging trends,” Immunology and Cell Biology, vol. 84, no. 4, pp. 333–341, 2006.
[147]
A. Baumert, R. M. Bruckmaier, and O. Wellnitz, “Dose dependant SCC changes after intramammary lipopoly-saccharide challenge,” Milchwissenschaft, vol. 64, no. 2, pp. 119–121, 2009.
[148]
J. A. Mount, N. A. Karrow, J. L. Caswell, H. J. Boermans, and K. E. Leslie, “Assessment of bovine mammary chemokine gene expression in response to lipopolysaccharide, lipotechoic acid + peptidoglycan, and CpG oligodeoxynucleotide 2135,” Canadian Journal of Veterinary Research, vol. 73, no. 1, pp. 49–57, 2009.
[149]
S. Schmitz, M. W. Pfaffl, H. H. D. Meyer, and R. M. Bruckmaier, “Short-term changes of mRNA expression of various inflammatory factors and milk proteins in mammary tissue during LPS-induced mastitis,” Domestic Animal Endocrinology, vol. 26, no. 2, pp. 111–126, 2004.
[150]
N. Isobe, K. Morimoto, J. Nakamura, A. Yamasaki, and Y. Yoshimura, “Intramammary challenge of lipopolysaccharide stimulates secretion of lingual antimicrobial peptide into milk of dairy cows,” Journal of Dairy Science, vol. 92, no. 12, pp. 6046–6051, 2009.
[151]
R. Pareek, O. Wellnitz, R. van Dorp, J. Burton, and D. Kerr, “Immunorelevant gene expression in LPS-challenged bovine mammary epithelial cells,” Journal of Applied Genetics, vol. 46, no. 2, pp. 171–177, 2005.
[152]
O. Wellnitz, E. T. Arnold, and R. M. Bruckmaier, “Lipopolysaccharide and lipoteichoic acid induce different immune responses in the bovine mammary gland,” Journal of Dairy Science, vol. 94, no. 11, pp. 5405–5412, 2011.
[153]
Y. Wang, D. S. Zarlenga, M. J. Paape, and G. E. Dahl, “Recombinant bovine soluble CD14 sensitizes the mammary gland to lipopolysaccharide,” Veterinary Immunology and Immunopathology, vol. 86, no. 1-2, pp. 115–124, 2002.
[154]
S. E. Girardin, I. G. Boneca, L. A. M. Carneiro et al., “Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan,” Science, vol. 300, no. 5625, pp. 1584–1587, 2003.
[155]
B. Dogan, S. Klaessig, M. Rishniw et al., “Adherent and invasive Escherichia coli are associated with persistent bovine mastitis,” Veterinary Microbiology, vol. 116, no. 4, pp. 270–282, 2006.
[156]
J. B. Wardenburg, W. A. Williams, and D. Missiakas, “Host defenses against Staphylococcus aureus infection require recognition of bacterial lipoproteins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 37, pp. 13831–13836, 2006.
[157]
S. E. Girardin, L. H. Travassos, M. Hervé et al., “Peptidoglycan molecular requirements allowing detection by Nod1 and Nod2,” The Journal of Biological Chemistry, vol. 278, no. 43, pp. 41702–41708, 2003.
[158]
L. Sutra and B. Poutrel, “Virulence factors involved in the pathogenesis of bovine intramammary infections due to Staphylococcus aureus,” Journal of Medical Microbiology, vol. 40, no. 2, pp. 79–89, 1994.
[159]
S. Morath, A. Stadelmaier, A. Geyer, R. R. Schmidt, and T. Hartung, “Synthetic lipoteichoic acid from Staphylococcus aureus is a potent stimulus of cytokine release,” Journal of Experimental Medicine, vol. 195, no. 12, pp. 1635–1640, 2002.
[160]
R. Schwandner, R. Dziarski, H. Wesche, M. Rothe, and C. J. Kirschning, “Peptidoglycan- and lipoteichoic acid-induced cell activation is mediated by Toll-like receptor 2,” Journal of Biological Chemistry, vol. 274, no. 25, pp. 17406–17409, 1999.
[161]
P. Rainard, A. Fromageau, P. Cunha, and F. B. Gilbert, “Staphylococcus aureus lipoteichoic acid triggers inflammation in the lactating bovine mammary gland,” Veterinary Research, vol. 39, article 52, no. 5, 2008.
[162]
S. Bougarn, P. Cunha, F. B. Gilbert, A. Harmache, G. Foucras, and P. Rainard, “Staphylococcal-associated molecular patterns enhance expression of immune defense genes induced by IL-17 in mammary epithelial cells,” Cytokine, vol. 56, no. 3, pp. 749–759, 2011.
[163]
K. A. Daly, S. L. Mailer, M. R. Digby et al., “Molecular analysis of tammar (Macropus eugenii) mammary epithelial cells stimulated with lipopolysaccharide and lipoteichoic acid,” Veterinary Immunology and Immunopathology, vol. 129, no. 1-2, pp. 36–48, 2009.
[164]
E. T. Reitschel, T. Kirikae, F. U. Shade et al., “Bacterial endotoxin: molecular relationships of structure to activity and function,” FASEB Journal, vol. 8, no. 2, pp. 217–225, 1994.
[165]
D. D. Bannerman, M. J. Paape, J. W. Lee, X. Zhao, J. C. Hope, and P. Rainard, “Escherichia coli and Staphylococcus aureus elicit differential innate immune responses following intramammary infection,” Clinical and Diagnostic Laboratory Immunology, vol. 11, no. 3, pp. 463–472, 2004.
[166]
T. Kawai and S. Akira, “The role of pattern-recognition receptors in innate immunity: update on toll-like receptors,” Nature Immunology, vol. 11, no. 5, pp. 373–384, 2010.
[167]
L. H. Travassos, S. E. Girardin, D. J. Philpott et al., “Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition,” EMBO Reports, vol. 5, no. 10, pp. 1000–1006, 2004.
[168]
G. Mancuso, M. Gambuzza, A. Midiri et al., “Bacterial recognition by TLR7 in the lysosomes of conventional dendritic cells,” Nature Immunology, vol. 10, no. 6, pp. 587–594, 2009.
[169]
K. A. Zarember and P. J. Godowski, “Tissue expression of human Toll-like receptors and differential regulation of Toll-like receptor mRNAs in leukocytes in response to microbes, their products, and cytokines,” Journal of Immunology, vol. 168, no. 2, pp. 554–561, 2002.
[170]
F. R. Buzzola, L. P. Alvarez, L. P. N. Tuchscherr et al., “Differential abilities of capsulated and noncapsulated Staphylococcus aureus isolates from diverse agr groups to invade mammary epithelial cells,” Infection and Immunity, vol. 75, no. 2, pp. 886–891, 2007.
[171]
S. Hensen, M. Pavi？i？, J. Lohuis, and B. Poutrel, “Use of bovine primary mammary epithelial cells for the comparison of adherence and invasion ability of Staphylococcus aureus strains,” Journal of Dairy Science, vol. 83, no. 3, pp. 418–429, 2000.
[172]
M. Sorensen and S. Sorensen, “The proteins in whey,” Comptes Rendus des Travaux du Laboratoire Carlsberg Série: Chimiqu, vol. 23, no. 7, pp. 55–99, 1940.
[173]
K. Persson, A. Carlsson, C. Hambleton, and A. J. Guidry, “Immunoglobulins, lysozyme and lactoferrin in the teat and udder of the dry cow during endotoxin-induced inflammation,” Journal of Veterinary Medicine B, vol. 39, no. 3, pp. 165–174, 1992.
[174]
A. J. Molenaar, Y. M. Kuys, S. R. Davis, R. J. Wilkins, P. E. Mead, and J. W. Tweedie, “Elevation of lactoferrin gene expression in developing, ductal, resting, and regressing parenchymal epithelium of the ruminant mammary gland,” Journal of Dairy Science, vol. 79, no. 7, pp. 1198–1208, 1996.
[175]
F. L. Schanbacher, R. E. Goodman, and R. S. Talhouk, “Bovine mammary lactoferrin: implications from messenger ribonucleic acid (mRNA) sequence and regulation contrary to other milk proteins,” Journal of Dairy Science, vol. 76, no. 12, pp. 3812–3831, 1993.
[176]
S.-I. Hagiwara, K. Kawai, A. Anri, and H. Nagahata, “Lactoferrin concentrations in milk from normal and subclinical mastitic cows,” Journal of Veterinary Medical Science, vol. 65, no. 3, pp. 319–323, 2003.
[177]
B. Reiter, “Review of the progress of dairy science: antimicrobial systems in milk,” Journal of Dairy Research, vol. 45, no. 1, pp. 131–147, 1978.
[178]
J. B. Cheng, J. Q. Wang, D. P. Bu et al., “Factors affecting the lactoferrin concentration in bovine milk,” Journal of Dairy Science, vol. 91, no. 3, pp. 970–976, 2008.
[179]
K. L. Smith and S. P. Oliver, “Lactoferrin: a component of nonspecific defense of the involuting bovine mammary gland,” Advances in Experimental Medicine and Biology, vol. 137, pp. 535–554, 1981.
[180]
P. Rainard, “Experimental mastitis with Escherichia coli: kinetics of bacteriostatic and bactericidal activities,” Annales de Recherches Veterinaires, vol. 14, no. 1, pp. 1–11, 1983.
[181]
D. Todhunter, K. L. Smith, and J. S. Hogan, “Intramammary challenge of the bovine mammary gland with coliform bacteria during early involution,” Journal of Dairy Science, vol. 73, no. 5, pp. 1217–1224, 1990.
[182]
J. H. Nuijens, P. H. van Berkel, and F. L. Schanbacher, “Structure and biological actions of lactoferrin,” Journal of Mammary Gland Biology and Neoplasia, vol. 1, no. 3, pp. 285–295, 1996.
[183]
P. P. Ward, S. Uribe-Luna, and O. M. Conneely, “Lactoferrin and host defense,” Biochemistry and Cell Biology, vol. 80, no. 1, pp. 95–102, 2002.
[184]
D. A. Clare and H. E. Swaisgood, “Bioactive milk peptides: a prospectus,” Journal of Dairy Science, vol. 83, no. 6, pp. 1187–1195, 2000.
[185]
J. Erdei, A. Forsgren, and A. S. Naidu, “Lactoferrin binds to porins OmpF and OmpC in Escherichia coli,” Infection and Immunity, vol. 62, no. 4, pp. 1236–1240, 1994.
[186]
M. S. Diarra, D. Petitclerc, and P. Lacasse, “Effect of lactoferrin in combination with penicillin on the morphology and the physiology of Staphylococcus aureus isolated from bovine mastitis,” Journal of Dairy Science, vol. 85, no. 5, pp. 1141–1149, 2002.
[187]
R. T. Ellison III, Q. Luo, and L. B. Reller, “Enhancement of the activity of cefotaxime by iron-binding proteins,” Journal of Antimicrobial Chemotherapy, vol. 25, no. 3, pp. 479–481, 1990.
[188]
R. T. Ellison III, T. J. Giehl, and F. M. LaForce, “Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin,” Infection and Immunity, vol. 56, no. 11, pp. 2774–2781, 1988.
[189]
I. Moshynskyy, M. Jiang, M. C. Fontaine, J. Perez-Casal, L. A. Babiuk, and A. A. Potter, “Characterization of a bovine lactoferrin binding protein of Streptococcus uberis,” Microbial Pathogenesis, vol. 35, no. 5, pp. 203–215, 2003.
[190]
P. Rainard, “Binding of bovine lactoferrin to Streptococcus agalactiae,” FEMS Microbiology Letters, vol. 98, no. 1–3, pp. 235–239, 1992.
[191]
A. S. Naidu, M. Andersson, J. Miedzobrodzki, A. Forsgren, and J. L. Watts, “Bovine lactoferrin receptors in Staphylococcus aureus isolated from bovine mastitis,” Journal of Dairy Science, vol. 74, no. 4, pp. 1218–1226, 1991.
[192]
A. S. Naidu, J. Miedzobrodzki, M. Andersson, L.-E. Nilsson, A. Forsgren, and J. L. Watts, “Bovine lactoferrin binding to six species of coagulase-negative staphylococci isolated from bovine intramammary infections,” Journal of Clinical Microbiology, vol. 28, no. 10, pp. 2312–2319, 1990.
[193]
P. Hyv？nen, S. Kayhko, S. Taponen, A. von Wright, and S. Pyorala, “Effect of bovine lactoferrin on the internalization of coagulase-negative staphylococci into bovine mammary epithelial cells under in-vitro conditions,” Journal of Dairy Research, vol. 76, no. 2, pp. 144–151, 2009.
[194]
P. Rainard, “Bacteriostatic activity of bovine lactoferrin in mastitic milk,” Veterinary Microbiology, vol. 13, no. 2, pp. 159–166, 1987.
[195]
P. Rainard, “Bacteriostasis of Escherichia coli by bovine lactoferrin, transferrin and immunoglobulins (IgG1, IgG2, IgM) acting alone or in combination,” Veterinary Microbiology, vol. 11, no. 1-2, pp. 103–115, 1986.
[196]
K. M. Swanson, K. Stelwagen, J. Dobson et al., “Transcriptome profiling of Streptococcus uberis-induced mastitis reveals fundamental differences between immune gene expression in the mammary gland and in a primary cell culture model,” Journal of Dairy Science, vol. 92, no. 1, pp. 117–129, 2009.
[197]
L. Chaneton, L. Tirante, J. Maito, J. Chaves, and L. E. Bussmann, “Relationship between milk lactoferrin and etiological agent in the mastitic bovine mammary gland,” Journal of Dairy Science, vol. 91, no. 5, pp. 1865–1873, 2008.
[198]
W. Fang, R. A. Almeida, and S. P. Oliver, “Effects of lactoferrin and milk on adherence of Streptococcus uberis to bovine mammary epithelial cells,” American Journal of Veterinary Research, vol. 61, no. 3, pp. 275–279, 2000.
[199]
R. A. Almeida, D. A. Luther, H.-M. Park, and S. P. Oliver, “Identification, isolation, and partial characterization of a novel Streptococcus uberis adhesion molecule (SUAM),” Veterinary Microbiology, vol. 115, no. 1–3, pp. 183–191, 2006.
[200]
D. A. Dionysius and J. M. Milne, “Antibacterial peptides of bovine lactoferrin: purification and characterization,” Journal of Dairy Science, vol. 80, no. 4, pp. 667–674, 1997.
[201]
D. A. Dionysius, P. A. Grieve, and J. M. Milne, “Forms of lactoferrin: their antibacterial effect on enterotoxigenic Escherichia coli,” Journal of Dairy Science, vol. 76, no. 9, pp. 2597–2606, 1993.
[202]
D. R. Ambruso and R. B. Johnston Jr., “Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil particulate fractions, and enzymatic generating system,” Journal of Clinical Investigation, vol. 67, no. 2, pp. 352–360, 1981.
[203]
R. Oseas, H. H. Yang, R. L. Baehner, and L. A. Boxer, “Lactoferrin: a promoter of polymorphonuclear leukocyte adhesiveness,” Blood, vol. 57, no. 5, pp. 939–945, 1981.
[204]
K. Kai, K.-I. Komine, Y. Komine et al., “Lactoferrin stimulates a Staphylococcus aureus killing activity of bovine phagocytes in the mammary gland,” Microbiology and Immunology, vol. 46, no. 3, pp. 187–194, 2002.
[205]
H. E. Broxmeyer and E. Platzer, “Lactoferrin acts on I-A and I-E/C antigen subpopulations of mouse peritoneal macrophages in the absence of T lymphocytes and other cell types to inhibit production of granulocyte-macrophage colony stimulatory factors in vitro,” Journal of Immunology, vol. 133, no. 1, pp. 306–314, 1984.
[206]
H. E. Broxmeyer, A. Smithyman, R. R. Eger, P. A. Meyers, and M. de Sousa, “Identification of lactoferrin as the granulocyte-derived inhibitor of colony-stimulating activity production,” The Journal of Experimental Medicine, vol. 148, no. 4, pp. 1052–1067, 1978.
[207]
K. Kawai, S. Hagiwara, A. Anri, and H. Nagahata, “Lactoferrin concentration in milk of bovine clinical mastitis,” Veterinary Research Communications, vol. 23, no. 7, pp. 391–398, 1999.
[208]
P. Hyv？nen, L. Suojala, T. Orro et al., “Transgenic cows that produce recombinant human lactoferrin in milk are not protected from experimental Escherichia coli intramammary infection,” Infection and Immunity, vol. 74, no. 11, pp. 6206–6212, 2006.
[209]
O. Wellnitz, U. Berger, W. Schaeren, and R. M. Bruckmaier, “Mastitis severity induced by two Streptococcus uberis strains is refl ected by the mammary immune response in vitro,” Schweizer Archiv fur Tierheilkunde, vol. 154, no. 8, pp. 317–323, 2012.
[210]
B. J. Nonnecke and K. L. Smith, “Inhibition of mastitic bacteria by bovine milk apo-lactoferrin evaluated by in vitro microassay of bacterial growth,” Journal of Dairy Science, vol. 67, no. 3, pp. 606–613, 1984.
[211]
P. Rainard, “Bacteriostatic activity of bovine milk lactoferrin against mastitic bacteria,” Veterinary Microbiology, vol. 11, no. 4, pp. 387–392, 1986.
[212]
A. Pierce, D. Colavizza, M. Benaissa et al., “Molecular cloning and sequence analysis of bovine lactotransferrin,” European Journal of Biochemistry, vol. 196, no. 1, pp. 177–184, 1991.
[213]
B. Poutrel, P. Rainard, and J. P. Caffin, “Lactoferrin and transferrin in bovine milk in relation to certain physiological and pathological factors,” Annales de Recherches Veterinaires, vol. 13, no. 4, pp. 321–328, 1982.
[214]
L. Sanchez, P. Aranda, M. D. Perez, and M. Calvo, “Concentration of lactoferrin and transferrin throughout lactation in cow's colostrum and milk,” Biological Chemistry Hoppe-Seyler, vol. 369, no. 9, pp. 1005–1008, 1988.
[215]
M. Ollivier-Bousquet, “Transferrin and prolactin transcytosis in the lactating mammary epithelial cell,” Journal of Mammary Gland Biology and Neoplasia, vol. 3, no. 3, pp. 303–313, 1998.
[216]
L. Pellegrino and A. Tirelli, “A sensitive HPLC method to detect hen's egg white lysozyme in milk and dairy products,” International Dairy Journal, vol. 10, no. 7, pp. 435–442, 2000.
[217]
S. Priyadarshini and V. K. Kansal, “Lysozyme activity in buffalo milk: effect of lactation period, parity, mastitis, season in India, pH and milk processing heat treatment,” Asian-Australasian Journal of Animal Sciences, vol. 15, no. 6, pp. 895–899, 2002.
[218]
E. C. Leitch and M. D. P. Willcox, “Elucidation of the antistaphylococcal action of lactoferrin and lysozyme,” Journal of Medical Microbiology, vol. 48, no. 9, pp. 867–871, 1999.
[219]
A. P. Soldatov and A. I. Lyumbimov, “Age related and seasonal variation of milk lysozyme activity in cows,” Soviet Agricultural Sciences, vol. 5, pp. 39–40, 1986.
[220]
H. Korhonen, “Antimicrobial factors in bovine colostrum [dairy cattle, milk and cream],” Journal of the Scientific Agricultural Society of Finland, vol. 49, pp. 434–447, 1977.
[221]
A. Pandya and G. F. Haenlein, “Bioactive components in buffalo milk,” in Bioactive Components in Milk and Dairy Products, W. P. Young, Ed., p. 105, Wiley Blackwell, Oxford, UK, 2009.
[222]
Y. A. Radwan and A. A. Elmarimi, “The use of lysoplate test in the diagnosis of subclinical mastitis,” Bulletin of Animal Health Production in Africa, vol. 35, pp. 100–135, 1987.
[223]
？. Carlsson, L. Bj？rck, and K. Persson, “Lactoferrin and lysozyme in milk during acute mastitis and their inhibitory effect in Delvotest P,” Journal of Dairy Science, vol. 72, no. 12, pp. 3166–3175, 1989.
[224]
S. Priyadarshini and V. K. Kansal, “Purification, characterization, antibacterial activity and N-terminal sequencing of buffalo-milk lysozyme,” Journal of Dairy Research, vol. 69, no. 3, pp. 419–431, 2002.
[225]
P. F. Fox and A. L. Kelly, “Indigenous enzymes in milk: overview and historical aspects—part 1,” International Dairy Journal, vol. 16, no. 6, pp. 500–516, 2006.
[226]
H. Korhonen and A. Pihlanto, “Bioactive peptides from food proteins,” in Handbook of Food Products Manufacturing: Health, Meat, Milk, Poultry, Seafood, and Vegetables, Y. Hui, Ed., pp. 5–38, John Wiley & Sons, Hoboken, NJ, USA, 2007.
[227]
H. Korhonen and A. Pihlanto, “Food-derived bioactive peptides—opportunities for designing future foods,” Current Pharmaceutical Design, vol. 9, no. 16, pp. 1297–1308, 2003.
[228]
P. F. Fox, “Significance of indigenous enzymes in milk and dairy products,” in Handbook of Food Enzymology, pp. 255–278, Marcel Dekker, New York, NY, USA, 2003.
[229]
E. Seifu, E. F. Donkin, and E. M. Buys, “Potential of lactoperoxidase to diagnose subclinical mastitis in goats,” Small Ruminant Research, vol. 69, no. 1-3, pp. 154–158, 2007.
[230]
R. Cooray and L. Bj？rck, “Bactericidal activity of the bovine myeloperoxidase system against bacteria associated with mastitis,” Veterinary Microbiology, vol. 46, no. 4, pp. 427–434, 1995.
[231]
R. Cooray, “Use of bovine myeloperoxidase as an indicator of mastitis in dairy cattle,” Veterinary Microbiology, vol. 42, no. 4, pp. 317–326, 1994.
[232]
S. J. Klebanoff, “Myeloperoxidase: occurrence and biological function,” in Peroxidases in Chemistry and Biology, vol. 1, pp. 1–35, CRC Press, Boca Raton, Fla, USA, 1991.
[233]
P. Rainard, “The complement in milk and defense of the bovine mammary gland against infections,” Veterinary Research, vol. 34, no. 5, pp. 647–670, 2003.
[234]
M. M. Frank and L. F. Fries, “The role of complement in inflammation and phagocytosis,” Immunology Today, vol. 12, no. 9, pp. 322–326, 1991.
[235]
D. E. Shuster, M. E. Kehrli Jr., P. Rainard, and M. Paape, “Complement fragment C5a and inflammatory cytokines in neutrophil recruitment during intramammary infection with Escherichia coli,” Infection and Immunity, vol. 65, no. 8, pp. 3286–3292, 1997.
[236]
K. Reid, “The complement system; a major effector mechanism in humoral immunity,” Immunologist, vol. 3, pp. 206–208, 1995.
[237]
J. H. Brock, F. Ortega, and A. Pineiro, “Bactericidal and haemolytic activity of complement in bovine colostrum and serum: effect of proteolytic enzymes and ethylene glycol tetraacetic acid (EGTA),” Annales d'Immunologie, vol. 126, no. 4, pp. 439–451, 1975.
[238]
P. Rainard, B. Poutrel, and J. P. Caffin, “Assessment of hemolytic and bactericidal complement activities in normal and mastitic bovine milk,” Journal of Dairy Science, vol. 67, no. 3, pp. 614–619, 1984.
[239]
C. Riollet, P. Rainard, and B. Poutrel, “Differential induction of complement fragment C5a and inflammatory cytokines during intramammary infections with Escherichia coli and Staphylococcus aureus,” Clinical and Diagnostic Laboratory Immunology, vol. 7, no. 2, pp. 161–167, 2000.
[240]
W. P. Eckblad, K. M. Hendrix, and D. P. Olson, “Total complement hemolytic activity of colostral whey and sera from dairy cows,” The Cornell Veterinarian, vol. 71, no. 1, pp. 54–58, 1981.
[241]
P. Rainard and B. Poutrel, “Deposition of complement components on Streptococcus agalactiae in bovine milk in the absence of inflammation,” Infection and Immunity, vol. 63, no. 9, pp. 3422–3427, 1995.
[242]
P. Rainard, P. Sarradin, M. J. Paape, and B. Poutrel, “Quantification of C5a/C5a(desArg) in bovine plasma, serum and milk,” Veterinary Research, vol. 29, no. 1, pp. 73–88, 1998.
[243]
R. Mueller, E. J. Carroll, and L. Panico, “Complement C3 levels and haemolytic activity in normal and mastitic whey,” Zentralblatt für Veterinarmedizin B, vol. 29, no. 2, pp. 99–106, 1982.
[244]
R. Mueller, E. J. Carroll, and L. Panico, “Hemolytic complement titers and complement C3 levels in endotoxin-induced mastitis,” The American Journal of Veterinary Research, vol. 44, no. 8, pp. 1442–1445, 1983.
[245]
P. Rainard, P. Sarradin, and B. Poutrel, “Phenotypic variability of X-protein expression by mastitis-causing Streptococcus agalactiae of serotype NT/X and opsonic activities of specific antibodies,” Microbial Pathogenesis, vol. 16, no. 5, pp. 359–372, 1994.
[246]
L. Y. L. Lee, M. H？？k, D. Haviland et al., “Inhibition of complement activation by a secreted Staphylococcus aureus protein,” Journal of Infectious Diseases, vol. 190, no. 3, pp. 571–579, 2004.
[247]
H. Korhonen, P. Marnila, and H. S. Gill, “Milk immunoglobulins and complement factors,” British Journal of Nutrition, vol. 84, no. 1, pp. S75–S80, 2000.
[248]
P. Rainard and B. Poutrel, “Generation of complement fragment C5a in milk is variable among cows,” Journal of Dairy Science, vol. 83, no. 5, pp. 945–951, 2000.
[249]
T. Taniguchi, “Cytokine signaling through nonreceptor protein tyrosine kinases,” Science, vol. 268, no. 5208, pp. 251–255, 1995.
[250]
D. J. Hall, C. Brownlee, and C. D. Stiles, “Interleukin-1 is a potent regulator of JE and KC gene expression in quiescent BALB/c fibroblasts,” Journal of Cellular Physiology, vol. 141, no. 1, pp. 154–159, 1989.
[251]
A. M. Alluwaimi and J. S. Cullor, “Cytokines gene expression patterns of bovine milk during middle and late stages of lactation,” Journal of Veterinary Medicine, Series B, vol. 49, no. 2, pp. 105–110, 2002.
[252]
C. M. Leutenegger, A. M. Alluwaimi, W. L. Smith, L. Perani, and J. S. Cullor, “Quantitation of bovine cytokine mRNA in milk cells of healthy cattle by real-time TaqMan polymerase chain reaction,” Veterinary Immunology and Immunopathology, vol. 77, no. 3-4, pp. 275–287, 2000.
[253]
S. Redpath, P. Ghazal, and N. R. J. Gascoigne, “Hijacking and exploitation of IL-10 by intracellular pathogens,” Trends in Microbiology, vol. 9, no. 2, pp. 86–92, 2001.
[254]
G. Trinchieri, “Cytokines acting on or secreted by macrophages during intracellular infection (IL-10, IL-12, IFN-γ),” Current Opinion in Immunology, vol. 9, no. 1, pp. 17–23, 1997.
[255]
K. Persson-Waller, I. G. Colditz, and H.-F. Seow, “Accumulation of leucocytes and cytokines in the lactating ovine udder during mastitis due to Staphylococcus aureus and Escherichia coli,” Research in Veterinary Science, vol. 62, no. 1, pp. 63–66, 1997.
[256]
D. D. Bannerman, “Pathogen-dependent induction of cytokines and other soluble inflammatory mediators during intramammary infection of dairy cows,” Journal of Animal Science, vol. 87, no. 13, pp. 10–25, 2009.
[257]
L. A. Babiuk, L. M. Sordillo, M. Campos, H. P. Hughes, A. Rossi-Campos, and R. Harland, “Application of interferons in the control of infectious diseases of cattle,” Journal of Dairy Science, vol. 74, no. 12, pp. 4385–4398, 1991.
[258]
G. M. Pighetti and L. M. Sordillo, “Enhanced antigen-specific responses in bovine mammary glands following administration of interleukin-2,” Journal of Dairy Science, vol. 78, no. 3, pp. 528–537, 1995.
[259]
G. M. Pighetti and L. M. Sordillo, “Specific immune responses of dairy cattle after primary inoculation with recombinant bovine interferon-γ as an adjuvant when vaccinating against mastitis,” American Journal of Veterinary Research, vol. 57, no. 6, pp. 819–824, 1996.
[260]
D. Goodson, M. Baca, and L. Babiuk, “Applications of bovine cytokines,” in Cytokines in Veterinary Medicine, V. E. Schijns and M. C. Horzinek, Eds., pp. 3–13, CAB International, New York, NY, USA, 1997.
[261]
R. J. Erskine, P. C. Bartlett, S. R. Tavernier et al., “Recombinant bovine interleukin-2 and dry cow therapy: efficacy to cure and prevent intramammary infections, safety, and effect on gestation,” Journal of Dairy Science, vol. 81, no. 1, pp. 107–115, 1998.
[262]
M. Daley, T. Williams, P. Coyle, G. Furda, R. Dougherty, and P. Hayes, “Prevention and treatment of Staphylococcus aureus infections with recombinant cytokines,” Cytokine, vol. 5, no. 3, pp. 276–284, 1993.
[263]
S. C. Nickerson, W. E. Owens, and J. L. Watts, “Effects of recombinant granulocyte colony-stimulating factor on Staphylococcus aureus mastitis in lactating dairy cows,” Journal of Dairy Science, vol. 72, no. 12, pp. 3286–3294, 1989.
[264]
L. M. Sordillo and L. A. Babiuk, “Controlling acute Escherichia coli mastitis during the periparturient period with recombinant bovine interferon gamma,” Veterinary Microbiology, vol. 28, no. 2, pp. 189–198, 1991.
[265]
M. J. Daley, G. Furda, R. Dougherty, P. A. Coyle, T. J. Williams, and P. Johnston, “Potentiation of antibiotic therapy for bovine mastitis by recombinant bovine interleukin-2,” Journal of dairy science, vol. 75, no. 12, pp. 3330–3338, 1992.
[266]
M. J. Daley, P. A. Coyle, T. J. Williams, G. Furda, R. Dougherty, and P. W. Hayes, “Staphylococcus aureus Mastitis: pathogenesis and treatment with bovine lnterleukin-1β and lnterleukin-2,” Journal of Dairy Science, vol. 74, no. 12, pp. 4413–4424, 1991.
[267]
M. S. Sanchez, C. W. Ford, and R. J. Yancey Jr., “Effect of tumor necrosis factor-alpha, interleukin-1 beta, and antibiotics on the killing of intracellular Staphylococcus aureus,” Journal of Dairy Science, vol. 77, no. 5, pp. 1251–1258, 1994.
[268]
P. G. Reddy, D. N. Reddy, S. E. Pruiett et al., “Interleukin 2 treatment of Staphylococcus aureus mastitis,” Cytokine, vol. 4, no. 3, pp. 227–231, 1992.
[269]
G. H. Quiroga, L. M. Sordillo, R. W. Adkinson, and S. C. Nickerson, “Cytologic responses of Staphylococcus aureus-infected mammary glands of heifers to interferon gamma and interleukin-2 treatment,” The American Journal of Veterinary Research, vol. 54, no. 11, pp. 1894–1900, 1993.
[270]
J. S. Hogan, K. L. Smith, D. A. Todhunter, P. S. Schoenberger, and D. Shuster, “Efficacy of recombinant bovine interleukin-2 as an adjunct to dry cow therapy,” Journal of Dairy Science, vol. 78, no. 5, pp. 1062–1067, 1995.
[271]
S. C. Nickerson, W. E. Owens, J. J. Rejman, and S. P. Oliver, “Effects of interleukin-1 and interleukin-2 on mammary gland leukocyte populations and histology during the early nonlactating period,” Journal of Veterinary Medicine B, vol. 40, no. 9-10, pp. 621–633, 1993.
[272]
D. N. Wedlock, M. Denis, J. Lacy-Hulbert, and B. M. Buddle, “Interleukin-1β infusion in bovine mammary glands prior to challenge with Streptococcus uberis reduces bacterial growth but causes sterile mastitis,” Veterinary Research Communications, vol. 32, no. 6, pp. 439–447, 2008.
[273]
A. M. Cole, T. Ganz, A. M. Liese, M. D. Burdick, L. Liu, and R. M. Strieter, “Cutting edge: IFN-inducible ELR-CXC chemokines display defensin-like antimicrobial activity,” Journal of Immunology, vol. 167, no. 2, pp. 623–627, 2001.
[274]
H. Lahouassa, P. Rainard, A. Caraty, and C. Riollet, “Identification and characterization of a new interleukin-8 receptor in bovine species,” Molecular Immunology, vol. 45, no. 4, pp. 1153–1164, 2008.
[275]
D. D. Bannerman, M. J. Paape, W. R. Hare, and J. C. Hope, “Characterization of the bovine innate immune response to intramammary infection with Klebsiella pneumoniae,” Journal of Dairy Science, vol. 87, no. 8, pp. 2420–2432, 2004.
[276]
P. Cormican, K. G. Meade, S. Cahalane et al., “Evolution, expression and effectiveness in a cluster of novel bovine β-defensins,” Immunogenetics, vol. 60, no. 3-4, pp. 147–156, 2008.
[277]
D. Yang, O. Chertov, S. N. Bykovskaia et al., “β-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6,” Science, vol. 286, no. 5439, pp. 525–528, 1999.
[278]
J. Tetens, J. J. Friedrich, A. Hartmann, M. Schwerin, E. Kalm, and G. Thaller, “The spatial expression pattern of antimicrobial peptides across the healthy bovine udder,” Journal of Dairy Science, vol. 93, no. 2, pp. 775–783, 2010.
[279]
G. Diamond, M. Zasloff, H. Eck, M. Brasseur, W. L. Maloy, and C. L. Bevins, “Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA,” Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 9, pp. 3952–3956, 1991.
[280]
L. M. Sordillo and S. C. Nickerson, “Quantification and immunoglobulin classification of plasma cells in nonlactating bovine mammary tissue.,” Journal of dairy science, vol. 71, no. 1, pp. 84–91, 1988.
[281]
C. Burvenich, G. V.-V. Messom, and A. W. Hill, “New insights into pathogenesis of mastitis,” Flemish Veterinary Journal, p. 236, 1991.
[282]
H. J. Korhonen, “Bioactive components in bovine milk,” in Bioactive Components in Milk and Dairy Products, W. P. Young, Ed., pp. 15–42, Wiley, Ames, Iowa, USA, 2009.
[283]
A. J. Guidry, M. J. Paape, and R. E. Pearson, “Effect of udder inflammation on milk immunoglobulins and phagocytosis,” American Journal of Veterinary Research, vol. 41, no. 5, pp. 751–753, 1980.
[284]
A. Musoke, F. Rurangirwa, and V. Nantulya, “Biological properties of bovine immunoglobulins and systemic antibody responses,” in The Ruminant Immune System Health and Disease, pp. 391–408, Cambridge University Press, Cambridge, UK, 1986.
[285]
E. Wilson and E. C. Butcher, “CCL28 controls immunoglobulin (Ig)A plasma cell accumulation in the lactating mammary gland and IgA antibody transfer to the neonate,” The Journal of Experimental Medicine, vol. 200, no. 6, pp. 805–809, 2004.
[286]
J. E. Butler, “Bovine immunoglobulins: an augmented review,” Veterinary Immunology and Immunopathology, vol. 4, no. 1-2, pp. 43–152, 1983.
[287]
T. J. Newby and J. Bourne, “The nature of the local immune system of the bovine mammary gland,” Journal of Immunology, vol. 118, no. 2, pp. 461–465, 1977.
[288]
J. E. Butler, C. F. Maxwell, C. S. Pierce, M. B. Hylton, R. Asofsky, and C. A. Kiddy, “Studies on the relative synthesis and distribution of IgA and IgG1 in various tissues and body fluids of the cow,” Journal of Immunology, vol. 109, no. 1, pp. 38–46, 1972.
[289]
G. M. Barrington, T. E. Besser, W. C. Davis, C. C. Gay, J. J. Reeves, and T. B. McFadden, “Expression of immunoglobulin G1 receptors by bovine mammary epithelial cells and mammary leukocytes,” Journal of Dairy Science, vol. 80, no. 1, pp. 86–93, 1997.
[290]
C. S. Lee and A. K. Lascelles, “Antibody-producing cells in antigenically stimulated mammary glands and in the gastro-intestinal tract of sheep,” The Australian Journal of Experimental Biology and Medical Science, vol. 48, no. 5, pp. 525–535, 1970.
[291]
A. Harada, N. Sekido, T. Akahoshi, T. Wada, N. Mukaida, and K. Matsushima, “Essential involvement of interleukin-8 (IL-8) in acute inflammation,” Journal of Leukocyte Biology, vol. 56, no. 5, pp. 559–564, 1994.
[292]
Y. Kobayashi, “The role of chemokines in neutrophil biology,” Frontiers in Bioscience, vol. 13, no. 7, pp. 2400–2407, 2008.
[293]
C. Dinarello, “Cytokines as mediators in the pathogenesis of septic shock,” in Pathology of Septic Shock, vol. 216 of Current Topics in Microbiology and Immunology, pp. 133–165, Springer, Berlin, Germany, 1996.
[294]
M. Laan, Z.-H. Cui, H. Hoshino, et al., “Neutrophil recruitment by human IL-17 via C-X-C chemokine release in the airways,” The Journal of Immunology, vol. 162, no. 4, pp. 2347–2352, 1999.
[295]
J. A. Hamilton, “Colony stimulating factors, cytokines and monocyte-macrophages—some controversies,” Immunology Today, vol. 14, no. 1, pp. 18–24, 1993.
[296]
M. I. Cybulsky, D. J. McComb, and H. Z. Movat, “Neutrophil leukocyte emigration induced by endotoxin. Mediator roles of interleukin 1 and tumor necrosis factor α 1,” Journal of Immunology, vol. 140, no. 9, pp. 3144–3149, 1988.
[297]
A. R. Huber, S. L. Kunkel, R. F. Todd III, and S. J. Weiss, “Regulation of transendothelial neutrophil migration by endogenous interleukin-8,” Science, vol. 254, no. 5028, pp. 99–102, 1991.
[298]
M. K. Gately, L. M. Renzetti, J. Magram et al., “The interleukin-12/interleukin-12-receptor system: role in normal and pathologic immune responses,” Annual Review of Immunology, vol. 16, no. 1, pp. 495–521, 1998.
[299]
G. Trinchieri, “Interleukin-12 and the regulation of innate resistance and adaptive immunity,” Nature Reviews Immunology, vol. 3, no. 2, pp. 133–146, 2003.
[300]
E. T. Keller, J. Wanagat, and W. B. Ershler, “Molecular and cellular biology of interleukin-6 and its receptor,” Frontiers in Bioscience, vol. 1, pp. d340–d357, 1996.
[301]
T. van der Poll and S. J. van Deventer, “The role of interleukin 6 in endotoxin-induced inflammatory responses,” Progress in Clinical and Biological Research, vol. 397, pp. 365–377, 1998.
[302]
J. R. Schoenborn and C. B. Wilson, “Regulation of interferon-γ during innate and adaptive immune responses,” Advances in Immunology, vol. 96, pp. 41–101, 2007.
[303]
K. Schroder, P. J. Hertzog, T. Ravasi, and D. A. Hume, “Interferon-γ: an overview of signals, mechanisms and functions,” Journal of Leukocyte Biology, vol. 75, no. 2, pp. 163–189, 2004.
[304]
A. K. Sample and C. J. Czuprynski, “Priming and stimulation of bovine neutrophils by recombinant human interleukin-1 alpha and tumor necrosis factor,” Journal of Leukocyte Biology, vol. 49, no. 2, pp. 107–115, 1991.
[305]
M. J. Steinbeck and J. A. Roth, “Neutrophil activation by recombinant cytokines,” Reviews of Infectious Diseases, vol. 11, no. 4, pp. 549–568, 1989.
[306]
C. A. Dinarello, J. G. Cannon, J. Mancilla, I. Bishai, J. Lees, and F. Coceani, “Interleukin-6 as an endogenous pyrogen: induction of prostaglandin E2 in brain but not in peripheral blood mononuclear cells,” Brain Research, vol. 562, no. 2, pp. 199–206, 1991.
[307]
D. E. Shuster, M. E. Kehrli Jr., and M. G. Stevens, “Cytokine production during endotoxin-induced mastitis in lactating dairy cows,” American Journal of Veterinary Research, vol. 54, no. 1, pp. 80–85, 1993.
[308]
D. M. Steel and A. S. Whitehead, “The major acute phase reactants: C-reactive protein, serum amyloid P component and serum amyloid A protein,” Immunology Today, vol. 15, no. 2, pp. 81–88, 1994.
[309]
H. E. Barksby, S. R. Lea, P. M. Preshaw, and J. J. Taylor, “The expanding family of interleukin-1 cytokines and their role in destructive inflammatory disorders,” Clinical and Experimental Immunology, vol. 149, no. 2, pp. 217–225, 2007.
[310]
L. E. Jensen and A. S. Whitehead, “Regulation of serum amyloid A protein expression during the acute-phase response,” Biochemical Journal, vol. 334, no. 3, pp. 489–503, 1998.
[311]
A. Chockalingam, M. J. Paape, and D. D. Bannerman, “Increased milk levels of transforming growth factor-α, β1, and β2 during Escherichia coli-induced mastitis,” Journal of Dairy Science, vol. 88, no. 6, pp. 1986–1993, 2005.
[312]
K. Bry, “Epidermal growth factor and transforming growth factor-α enhance the interleukin-1- and tumor necrosis factor-stimulated prostaglandin E2 production and the interleukin-1 specific binding on amnion cells,” Prostaglandins, Leukotrienes and Essential Fatty Acids, vol. 49, no. 6, pp. 923–928, 1993.
[313]
M. C. Subauste and D. Proud, “Effects of tumor necrosis factor-α, epidermal growth factor and transforming growth factor-α on interleukin-8 production by, and human rhinovirus replication in, bronchial epithelial cells,” International Immunopharmacology, vol. 1, no. 7, pp. 1229–1234, 2001.
[314]
O. E. Sorensen, J. B. Cowland, K. Theilgaard-M？nch, L. Liu, T. Ganz, and N. Borregaard, “Wound healing and expression of antimicrobial peptides/polypeptides in human keratinocytes, a consequence of common growth factors,” Journal of Immunology, vol. 170, no. 11, pp. 5583–5589, 2003.
[315]
W. C. Brown, A. C. Rice-Ficht, and D. M. Estes, “Bovine type 1 and type 2 responses,” Veterinary Immunology and Immunopathology, vol. 63, no. 1-2, pp. 45–55, 1998.
[316]
D. F. Fiorentino, A. Zlotnik, P. Vieira et al., “IL-10 acts on the antigen-presenting cell to inhibit cytokine production by Th1 cells,” Journal of Immunology, vol. 146, no. 10, pp. 3444–3451, 1991.
[317]
M. E. Kehrli, J. L. Burton, B. J. Nonnecke, and E. K. Lee, “Effects of stress on leukocyte trafficking and immune responses: implications for vaccination,” Advances in Veterinary Medicine, vol. 41, pp. 61–81, 1999.
[318]
G. Trinchieri, “Interleukin-12: A proinflammatory cytokine with immunoregulatory functions that bridge innate resistance and antigen-specific adaptive immunity,” Annual Review of Immunology, vol. 13, pp. 251–276, 1995.
[319]
T. R. Mosmann and R. L. Coffman, “TH1 and TH2 cells: Different patterns of lymphokine secretion lead to different functional properties,” Annual Review of Immunology, vol. 7, no. 1, pp. 145–173, 1989.
[320]
P. T. Mehrotra, D. Wu, J. A. Crim, H. S. Mostowski, and J. P. Siegel, “Effects of IL-12 on the generation of cytotoxic activity in human CD8 T lymphocytes,” Journal of Immunology, vol. 151, no. 5, pp. 2444–2452, 1993.
[321]
R. A. Seder, W. E. Paul, M. M. Davis, and B. F. De St. Groth, “The presence of interleukin 4 during in vitro priming determines the lymphokine-producing potential of CD4+ T cells from T cell receptor transgenic mice,” Journal of Experimental Medicine, vol. 176, no. 4, pp. 1091–1098, 1992.
[322]
D. F. Fiorentino, A. Zlotnik, T. R. Mosmann, M. Howard, and A. O'Garra, “IL-10 inhibits cytokine production by activated macrophages,” Journal of Immunology, vol. 147, no. 11, pp. 3815–3822, 1991.
[323]
W. C. Brown, V. M. Woods, C. G. Chitko-McKown, S. M. Hash, and A. C. Rice-Ficht, “Interleukin-10 is expressed by bovine type 1 helper, type 2 helper, and unrestricted parasite-specific T-cell clones and inhibits proliferation of all three subsets in an accessory-cell-dependent manner,” Infection and Immunity, vol. 62, no. 11, pp. 4697–4708, 1994.
[324]
K. W. Moore, R. de Waal Malefyt, R. L. Coffman, and A. O'Garra, “Interleukin-10 and the interleukin-10 receptor,” Annual Review of Immunology, vol. 19, no. 1, pp. 683–765, 2001.
[325]
G. S. Ashcroft, “Bidirectional regulation of macrophage function by TGF-β,” Microbes and Infection, vol. 1, no. 15, pp. 1275–1282, 1999.
[326]
J. J. Letterio and A. B. Roberts, “Regulation of immune responses by TGF-β,” Annual Review of Immunology, vol. 16, pp. 137–161, 1998.
[327]
R. Derynck, “The physiology of transforming growth factor-α,” Advances in Cancer Research, vol. 58, pp. 27–52, 1991.
[328]
M. Shah, D. M. Foreman, and M. W. J. Ferguson, “Neutralising antibody to TGF-1,2 reduces cutaneous scarring in adult rodents,” Journal of Cell Science, vol. 107, no. 5, pp. 1137–1157, 1994.
[329]
J.-W. Lee, D. D. Bannerman, M. J. Paape, M.-K. Huang, and X. Zhao, “Characterization of cytokine expression in milk somatic cells during intramammary infections with Escherichia coli or Staphylococcus aureus by real-time PCR,” Veterinary Research, vol. 37, no. 2, pp. 219–229, 2006.
[330]
O. Wellnitz, P. Reith, S. C. Haas, and H. H. D. Meyer, “Immune relevant gene expression of mammary epithelial cells and their influence on leukocyte chemotaxis in response to different mastitis pathogens,” Veterinarni Medicina, vol. 51, no. 4, pp. 125–132, 2006.
[331]
Y. Schukken, M. Chuff, P. Moroni et al., “The “other” gram-negative bacteria in mastitis,” Veterinary Clinics of North America—Food Animal Practice, vol. 28, no. 2, pp. 239–256, 2012.
[332]
Y. Yokomizo, Y. Mori, Y. Shimoji et al., “Proliferative response and cytokine production of bovine peripheral blood mononuclear cells induced by the superantigens staphylococcal enterotoxins and toxic shock syndrome toxin-1,” The Journal of Veterinary Medical Science of Japan Society for Veterinary Science, vol. 57, no. 2, pp. 299–305, 1995.
[333]
L. Bj？rk, J. Andersson, M. Ceska, and U. Andersson, “Endotoxin and Staphylococcus aureus enterotoxin a induce different patterns of cytokines,” Cytokine, vol. 4, no. 6, pp. 513–519, 1992.
[334]
L. Sordillo and J. Peel, “Effect of interferon-gamma on the production of tumor necrosis factor during acute Escherichia coli mastitis,” Journal of dairy science, vol. 75, no. 8, pp. 2119–2125, 1992.
[335]
S. Kushibiki, K. Hodate, H. Shingu et al., “Metabolic and lactational responses during recombinant bovine tumor necrosis factor-α treatment in lactating cows,” Journal of Dairy Science, vol. 86, no. 3, pp. 819–827, 2003.
[336]
M. Rambeaud, R. A. Almeida, G. M. Pighetti, and S. P. Oliver, “Dynamics of leukocytes and cytokines during experimentally induced Streptococcus uberis mastitis,” Veterinary Immunology and Immunopathology, vol. 96, no. 3-4, pp. 193–205, 2003.
[337]
D. D. Bannerman, M. J. Paape, J. P. Goff, K. Kimura, J. D. Lippolis, and J. C. Hope, “Innate immune response to intramammary infection with Serratia marcescens and Streptococcus uberis,” Veterinary Research, vol. 35, no. 6, pp. 681–700, 2004.
[338]
P. Rainard and M. J. Paape, “Sensitization of the bovine mammary gland to Escherichia coli endotoxin,” Veterinary Research, vol. 28, no. 3, pp. 231–238, 1997.
[339]
M. J. Paape, P. M. Rautiainen, E. M. Lilius, C. E. Malstrom, and T. H. Elsasser, “Development of anti-bovine TNF-α mAb and ELISA for quantitating TNF-α in milk after intramammary injection of endotoxin,” Journal of Dairy Science, vol. 85, no. 4, pp. 765–773, 2002.
[340]
K. P. Waller, I. G. Colditz, P. Flapper, and H.-F. Seow, “Leukocyte and cytokine accumulation in the ovine teat and udder during endotoxin-induced inflammation,” Veterinary Research Communications, vol. 21, no. 2, pp. 101–115, 1997.
[341]
J. W. Blum, H. Dosogne, D. Hoeben et al., “Tumor necrosis factor-α and nitrite/nitrate responses during acute mastitis induced by Escherichia coli infection and endotoxin in dairy cows,” Domestic Animal Endocrinology, vol. 19, no. 4, pp. 223–235, 2000.
[342]
D. Hoeben, C. Burvenich, E. Trevisi et al., “Role of endotoxin and TNF-α in the pathogenesis of experimentally induced coliform mastitis in periparturient cows,” Journal of Dairy Research, vol. 67, no. 4, pp. 503–514, 2000.
[343]
J. A. Harp, T. E. Waters, J. P. Goff, D. D. Bannerman, and M. J. Paape, “Expression of lymphocyte homing and adhesion molecules during intramammary infection of cows with Serratia marcescens or Streptococcus uberis: correlation with bacterial colonization and clinical signs,” Veterinary Immunology and Immunopathology, vol. 109, no. 1-2, pp. 13–21, 2006.
[344]
D. J. Wilson, J. H. Kirk, R. D. Walker, and Q. W. Bosworth, “Serratia marcescens mastitis in a dairy herd,” Journal of the American Veterinary Medical Association, vol. 196, no. 7, pp. 1102–1105, 1990.
[345]
E. Power, “Gangrenous mastitis in dairy herds,” The Veterinary Record, vol. 153, no. 25, pp. 791–792, 2003.
[346]
Y. Ijiri, K. Matsumoto, R. Kamata et al., “Suppression of polymorphonuclear leucocyte chemotaxis by Pseudomonas aeruginosa elastase in vitro: a study of the mechanisms and the correlation with ring abscess in pseudomonal keratitis,” International Journal of Experimental Pathology, vol. 75, no. 6, pp. 441–451, 1994.
[347]
A. Kharazmi and H. Nielsen, “Inhibition of human monocyte chemotaxis and chemiluminescence by Pseudomonas aeruginosaelastase,” Apmis, vol. 99, no. 1, pp. 93–95, 1991.
[348]
Y. Naiki, K. S. Michelsen, W. Zhang, S. Chen, T. M. Doherty, and M. Arditi, “Transforming growth factor-β differentially inhibits MyD88-dependent, but not TRAM- and TRIF-dependent, lipopolysaccharide-induced TLR4 signaling,” The Journal of Biological Chemistry, vol. 280, no. 7, pp. 5491–5495, 2005.
[349]
A. Brunmark and A. M. O'Rourke, “Augmentation of mature CD4+ T cell responses to isolated antigenic class II proteins by fibronectin and intercellular adhesion molecule-1,” Journal of Immunology, vol. 159, no. 4, pp. 1676–1685, 1997.
[350]
A. M. Alluwaimi, C. M. Leutenegger, T. B. Farver, P. V. Rossitto, W. L. Smith, and J. S. Cullor, “The cytokine markers in Staphylococcus aureus mastitis of bovine mammary gland,” Journal of Veterinary Medicine B, vol. 50, no. 3, pp. 105–111, 2003.
[351]
N. R. Benites, J. L. Guerra, P. A. Melville, and E. O. da Costa, “Aetiology and histopathology of bovine mastitis of espontaneous occurrence,” Journal of Veterinary Medicine, Series B, vol. 49, no. 8, pp. 366–370, 2002.
[352]
Y. de Haas, R. F. Veerkamp, H. W. Barkema, Y. T. Gr？hn, and Y. H. Schukken, “Associations between pathogen-specific cases of clinical mastitis and somatic cell count patterns,” Journal of Dairy Science, vol. 87, no. 1, pp. 95–105, 2004.
[353]
M. Chaffer, G. Leitner, M. Winkler, et al., “Coagulase-negative staphylococci and mammary gland infections in cows,” Journal of Veterinary Medicine Series B, vol. 46, no. 10, pp. 707–712, 1999.
[354]
H. Simojoki, T. Salom？ki, S. Taponen, A. Iivanainen, and S. Py？r？l？, “Innate immune response in experimentally induced bovine intramammary infection with Staphylococcus simulans and S. epidermidis,” Veterinary Research, vol. 42, no. 1, article 49, 2011.
[355]
P. Winter and I. G. Colditz, “Immunological responses of the lactating ovine udder following experimental challenge with Staphylococcus epidermidis,” Veterinary Immunology and Immunopathology, vol. 89, no. 1-2, pp. 57–65, 2002.
[356]
P. Winter, F. Schilcher, K. Fuchs, and I. G. Colditz, “Dynamics of experimentally induced Staphylococcus epidermidis mastitis in East Friesian milk ewes,” Journal of Dairy Research, vol. 70, no. 2, pp. 157–164, 2003.
[357]
H. Simojoki, T. Orro, S. Taponen, and S. Py？r？l？, “Host response in bovine mastitis experimentally induced with Staphylococcus chromogenes,” Veterinary Microbiology, vol. 134, no. 1-2, pp. 95–99, 2009.
[358]
A. R. Burriel, “Dynamics of intramammary infection in the sheep caused by coagulase-negative staphylococci and its influence on udder tissue and milk composition,” Veterinary Record, vol. 140, no. 16, pp. 419–423, 1997.
[359]
G. C. Fthenakis and J. E. T.Jones, “The effect of inoculation of coagulase-negative Staphylococci into the ovine mammary gland,” Journal of Comparative Pathology, vol. 102, no. 2, pp. 211–219, 1990.
[360]
M. Deinhofer and A. Pernthaner, “Staphylococcus spp. as mastitis-related pathogens in goat milk,” Veterinary Microbiology, vol. 43, no. 2-3, pp. 161–166, 1995.
[361]
C. Beecher, M. Daly, R. P. Ross, J. Flynn, T. V. McCarthy, and L. Giblin, “Characterization of the bovine innate immune response in milk somatic cells following intramammary infection with Streptococcus dysgalactiae subspecies dysgalactiae,” Journal of Dairy Science, vol. 95, no. 10, pp. 5720–5729, 2012.
[362]
K. M. Moyes, J. K. Drackley, D. E. Morin et al., “Gene network and pathway analysis of bovine mammary tissue challenged with Streptococcus uberis reveals induction of cell proliferation and inhibition of PPAR signaling as potential mechanism for the negative relationships between immune response and lipid metabolism,” BMC Genomics, vol. 10, article 542, 2009.
[363]
U. K. Berger, W. Schaeren, R. M. Bruckmaier, and O. Wellnitz, “Immune response of bovine mammary gland epithelial cells to two different strains of Streptococcus uberis,” in Proceedings of the Milchkonferenz, vol. 111, Vienna, Austria, 2009.
[364]
R. Tassi, T. N. McNeilly, J. L. Fitzpatrick et al., “Strain-specific pathogenicity of putative host-adapted and nonadapted strains of Streptococcus uberis in dairy cattle,” Journal of Dairy Science, vol. 96, no. 8, pp. 5129–5145, 2013.
[365]
L. H. Pedersen, B. Aalb？k, C. M. R？ntved et al., “Early pathogenesis and inflammatory response in experimental bovine mastitis due to Streptococcus uberis,” Journal of Comparative Pathology, vol. 128, no. 2-3, pp. 156–164, 2003.
[366]
L. H. Thomas, W. Haider, A. W. Hill, and R. S. Cook, “Pathologic findings of experimentally induced Streptococcus uberis infection in the mammary gland of cows,” The American Journal of Veterinary Research, vol. 55, no. 12, pp. 1723–1728, 1994.
[367]
M. Denis, S. J. Lacy-Hulbert, B. M. Buddle, J. H. Williamson, and D. N. Wedlock, “Streptococcus uberis-specific T cells are present in mammary gland secretions of cows and can be activated to kill S. uberis,” Veterinary Research Communications, vol. 35, no. 3, pp. 145–156, 2011.
[368]
G. Trigo, M. Dinis, ？. Fran？a et al., “Leukocyte populations and cytokine expression in the mammary gland in a mouse model of Streptococcus agalactiae mastitis,” Journal of Medical Microbiology, vol. 58, no. 7, pp. 951–958, 2009.
[369]
J. S. Cullor, N. Fairley, W. L. Smith et al., “Hemogram changes in lactating dairy cows given human recombinant granulocyte colony stimulating factor (r-MethuG-CSF),” Veterinary Pathology, vol. 27, no. 5, pp. 311–316, 1990.
[370]
L. M. Sordillo, M. Snider, H. Hughes, G. Afseth, M. Campos, and L. A. Babiuk, “Pathological changes in bovine mammary glands following intramammary infusion of recombinant lnterleukin-2,” Journal of Dairy Science, vol. 74, no. 12, pp. 4164–4174, 1991.
[371]
Y. W. Park, “Goat Milk; chemistry and nutrition,” in Handbook of Milk of Non Bovine Mammals, Y. W. Park and G. F. W. Haenlein, Eds., pp. 34–58, Blackwell, Ames, Iowa, USA, John Wiley & Sons, Oxford, UK, 2008.
[372]
F. Remeuf and J. Lenoir, “Relationship between the physico-chemical characteristics of goat's milk and its rennetability,” International Dairy Bulletin, vol. 202, p. 86, 1986.
[373]
E. Renner, Micronutrients in Milk and Milk-Based Food Products, Elsevier Applied Science, New York, NY, USA, 1989.
[374]
P. Marnila and H. Korhonen, “Immunoglobulins,” in Encyclopedia of Dairy Science, H. Roginski, J. W. Fuquay, and P. F. Fox, Eds., pp. 1950–1956, Academic Press, London, UK, 2002.
[375]
L. Elfstrand, H. Lindmark-M？nsson, M. Paulsson, L. Nyberg, and B. ？kesson, “Immunoglobulins, growth factors and growth hormone in bovine colostrum and the effects of processing,” International Dairy Journal, vol. 12, no. 11, pp. 879–887, 2002.
[376]
M. C. Goel and N. K. Kakker, “Quantitation of immunoglobulins (IgG, IgM and IgA) in serum and lacteal secretion of buffaloes (Bubalus bubalis),” Indian Journal of Animal Sciences, vol. 67, no. 7, pp. 559–562, 1997.
[377]
D. E. Shuster and M. E. Kehrli Jr., “Administration of recombinant human interleukin 1 receptor antagonist during endotoxin-induced mastitis in cows,” American Journal of Veterinary Research, vol. 56, no. 3, pp. 313–320, 1995.
