| Title: | "Molecular identification and expression analysis of a diapause hormone receptor in the corn earworm, Helicoverpa zea" |
| Author(s): | Zhang Q; Piermarini PM; Nachman RJ; Denlinger DL; |
| Address: | "Department of Entomology, Ohio State University, Columbus, OH, USA; Department of Evolution, Ecology and Organismal Biology, Ohio State University, 318 West 12th Avenue, Columbus, OH 43210, USA. Department of Entomology, Ohio State University, Ohio Agricultural Research and Development Center, 1680 Madison Avenue, Wooster, OH 44691, USA. Insect Control and Cotton Disease Research Unit, Southern Plains Agricultural Research Center, US Department of Agriculture-Agriculture Research Service, College Station, TX 77845, USA. Department of Entomology, Ohio State University, Columbus, OH, USA; Department of Evolution, Ecology and Organismal Biology, Ohio State University, 318 West 12th Avenue, Columbus, OH 43210, USA. Electronic address: Denlinger.1@osu.edu" |
| DOI: | 10.1016/j.peptides.2013.12.005 |
| ISSN/ISBN: | 1873-5169 (Electronic) 0196-9781 (Linking) |
| Abstract: | "Diapause hormone (DH) is an insect neuropeptide that is highly effective in terminating the overwintering pupal diapause in members of the Helicoverpa/Heliothis complex of agricultural pests, thus DH and related compounds have promise as tools for pest management. To augment our development of effective DH analogs and antagonists that could be used as diapause disruptors this study focuses on the cloning and identification of the DH receptor (DHR) in the corn earworm, Helicoverpa zea. The full-length dhr cDNA contains 2153 nucleotides encoding 511 amino acids. Our results suggest there are at least two splicing variants of Hezea-DHR. Hydrophobicity analysis and sequence alignment indicate that Hezea-DHR has 7 transmembrane regions and a highly conserved C-terminal region that is also present in related receptors. Hezea-DHR has 95%, 82% and 79% identity to a partial DHR sequence from Heliothis virescens, a full-length DHR in Orgyia thyellina, and DHR-1 in Bombyx mori, but only 45-49% identity to pheromone biosynthesis activating neuropeptide receptor (PBANR). Expression of dhr mRNA remained low in whole body extracts throughout diapause and in young nondiapausing pupae, but was distinctly elevated as development ensued in pharate adults 7 days after pupation. The highest expression of dhr mRNA we noted was in the ovary. A DHR fusion protein with enhanced-green fluorescent protein was successfully expressed heterologously in X. laevis oocytes, as verified by fluorescent imaging and Western blots, but an electrophysiological assay failed to detect receptor-ligand binding activity, which suggests that an essential cofactor and/or accessory protein is required for functional activity of the DHR" |
| Keywords: | "Animals Female Insect Proteins/genetics/*metabolism Moths/genetics/*metabolism Neuropeptides/genetics/*metabolism Oocytes/metabolism Ovary/metabolism RNA, Messenger/genetics Xenopus/metabolism Analogs Diapause hormone Diapause termination Receptor Xenopus;" |
| Notes: | "MedlineZhang, Qirui Piermarini, Peter M Nachman, Ronald J Denlinger, David L eng Research Support, U.S. Gov't, Non-P.H.S. 2013/12/19 Peptides. 2014 Mar; 53:250-7. doi: 10.1016/j.peptides.2013.12.005. Epub 2013 Dec 15" |
