|Title||Neuropeptides and peptide hormones identified in codling moth, Cydia pomonella (Lepidoptera: Tortricidae)|
|Publication Type||Journal Article|
|Year of Publication||2019|
|Authors||Garczynski, S, Hendrickson, C, Harper, A, Unruh, T, Dhingra, A, Ahn, S-J, Choi, M-Y|
|Journal||Archives of Insect Biochem. Physiol. (in press)|
|Keywords||codling moth, Neuropeptides, Proteomics, Transcriptome|
The codling moth, Cydia pomonella, is a worldwide pest of pome fruits. Neuropeptides regulate most physiological functions in insects, and represent new targets for development of control agents. The only neuropeptides reported from the codling moth to date are the allatostatin A family peptides. To identify other neuropeptides and peptide hormones from codling moth, we analyzed head transcriptomes, identified 50 transcripts, and predicted 120 prepropeptides for the codling moth neuropeptides and peptide hormones. All transcripts were amplified, and verified these sequences. One of notable findings in this study is that diapause hormones (DHs) reported from Tortricid moths including the codling moth do not have the WFGPRL sequence in C-terminal ends. The C-terminal motif is a critical to characterize insect DH peptides, and always conserved in pban/dh genes in Lepidoptera and many insect orders. Interestingly, the peptide sequence was produced only from the capa gene in the codling moth. The allatostatin A-family encoding transcript predicted 9 peptides, 7 of these peptides as expected are identical to those previously isolated from the moth. We also identified new codling moth orthologs of insect neuropeptides including CCHamides, allatostatin CC, RYamides and natalisins. The information provided in this study will benefit future codling moth investigations using peptidoproteomics to determine peptide presence and functions.