B. mori
not annotated - annotated - LINNAEUS only
21091811
Candidate chemosensory ionotropic receptors in a Lepidoptera.
A new family of candidate chemosensory ionotropic receptors (IRs) related to ionotropic glutamate receptors (iGluRs) was recently discovered in Drosophila melanogaster. Through Blast analyses of an expressed sequenced tag library prepared from male antennae of the noctuid moth Spodoptera littoralis, we identified 12 unigenes encoding proteins related to D. melanogaster and Bombyx mori IRs. Their full length sequences were obtained and the analyses of their expression patterns suggest that they were exclusively expressed or clearly enriched in chemosensory organs. The deduced protein sequences were more similar to B. mori and D. melanogaster IRs than to iGluRs and showed considerable variations in the predicted ligand-binding domains; none have the three glutamate-interacting residues found in iGluRs, suggesting different binding specificities. Our data suggest that we identified members of the insect IR chemosensory receptor family in S. littoralis and we report here the first demonstration of IR expression in Lepidoptera.
21199020
Genetic analysis of the xenobiotic resistance-associated ABC gene subfamilies of the Lepidoptera.
Some ATP-binding cassette (ABC) transporters of subfamilies B, C and G confer resistance to xenobiotics including insecticides. We identified genes of these subfamilies expressed by the lepidopterans Trichoplusia ni and Bombyx mori. The B. mori genome includes eight, six and 13 ABC-B, -C and -G genes, respectively, which encode P-glycoprotein, multidrug resistance protein, MRP, and breast cancer resistance protein, BCRP, homologues. Among the ABC-C and -G subfamilies, gene duplication contributes to protein diversity. We have identified three ABC-B and two ABC-C T. ni genes. Analyses of the T. ni MRP (TrnMRP) revealed unique features, including the potential for TrnMRP4 hyperglycosylation and the alternative splicing of TrnMRP1. Taken together, these attributes of moth multidrug resistance-associated ABCs may confer distinct functional capacities to xenobiotic efflux.