Renaming Bombyx mori Chemosensory Proteins

Based on these results, it certainly cannot be that CSPs are specifically tuned to chemosensory odor detection. We rather argue that CSPs play a key role in general lipid metabolism. This is a coherent argument to assent to the structure of the binding domain of CSPs (an open-air tube with long aliphatic chains ensheathed), the binding properties of these proteins towards lipids of all kinds, the huge repertoire of BmorCSP variants identified in the pheromone gland, their very general developmental and tissue-expression profiling as well as their insecticide response. It makes consistent the binding of cuticular hydrocarbons to ant CSPs [23]. It also makes consistent the existence of CSPs in aquatic arthropod species such as the water flea Daphnia pulex and the shrimp Artemia franciscana (ABH88167, ABH88166 and ABY62738). Chemosensory molecules detected by fleas and shrimps in the marine environment are necessarily very different than the highly volatile airborne chemosensory desaturated hydrocarbon pheromone odor chemical molecules perceived by insects in the terrestrial environment. In contrast, lipids are common to all arthropods from trilobites to ants and bees. BmorCSPs, H. virescens, moth, ant, bee, locust, whitefly, flea,shrimp CSPs and most probably also the whole and complete protein family should be renamed accordingly. This may help infer new functions to all CSP proteins, interpret the results in a new way independently of olfactory consideration and inspire science towards the discovery of the true function of this more and more intriguing insect-arthropod protein family