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Identification and characterization of a sex peptide receptor‐like transcript from the western tarnished plant bug L ygus hesperus
Author(s) -
Hull J. J.,
Brent C. S.
Publication year - 2014
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/imb.12082
Subject(s) - biology , hindgut , drosophila melanogaster , receptor , midgut , peptide , ligand (biochemistry) , insect , microbiology and biotechnology , biochemistry , botany , gene , larva
Lygus hesperus females exhibit a post‐mating behavioural switch that triggers increased egg laying and decreased sexual interest. In D rosophila melanogaster , these changes are controlled by sex peptide ( SP ) and the sex peptide receptor ( DmSPR ). In H elicoverpa armigera , SPR ( HaSPR ) also regulates some post‐mating behaviour; however, myoinhibiting peptides ( MIPs ) have been identified as the SPR ancestral ligand, indicating that SPR is a pleiotropic receptor. In the present study, we identified a transcript, designated L . hesperus SPR ( LhSPR ), that is homologous to known SPRs and which is expressed throughout development and in most adult tissues. Lh SPR was most abundant in female seminal depositories and heads as well as the hindgut/midgut of both sexes. In vitro analyses revealed that fluorescent chimeras of LhSPR , DmSPR and HaSPR localized to the cell surface of cultured insect cells, but only DmSPR and HaSPR bound carboxytetramethylrhodamine‐labelled analogues of D m SP 21–36 and DmMIP 4. Injected DmSP 21–36 also failed to have an effect on L . hesperus mating receptivity. Potential divergence in the LhSPR binding pocket may be linked to receptor‐ligand co‐evolution as 9 of 13 MIPs encoded by a putative L . hesperus MIP precursor exhibit an atypical W ‐ X 7 ‐ W amide motif vs the W ‐ X 6 ‐ W amide and W ‐ X 8 ‐ W amide motifs of D rosophila MIPs and SP .