Mouthparts enriched odorant binding protein AfasOBP11 plays a role in the gustatory perception of Adelphocoris fasciaticollis

J Insect Physiol. 2019 Aug-Sep:117:103915. doi: 10.1016/j.jinsphys.2019.103915. Epub 2019 Jul 20.

Abstract

Insect odorant binding proteins (OBPs), one of the most important groups of odor carriers, are believed to play essential roles in chemoreception. In the present study, we focused on AfasOBP11 in Adelphocoris fasciaticollis. Expression profiles showed that AfasOBP11 was mainly expressed in the mouthparts of A. fasciaticollis. Additionally, two types of sensilla, sensilla trichodeum and sensilla basiconicum, were found on the mouthparts of bugs. Moreover, anti-AfasOBP11 antiserum strongly labeled the sensilla basiconica. In fluorescence binding assays, recombinant AfasOBP11 displayed much stronger binding abilities to non-volatile secondary metabolite compounds than to volatile odors, suggesting a role of AfasOBP11 in taste sensing. To further investigate the biological functions of AfasOBP11, the feeding behavior of wild-type, dsGFP-injected and dsAfasOBP11-injected bugs was evaluated by performing electrical penetration graph (EPG) tests. After RNA interference of target AfasOBP11, A. fasciaticollis bugs spent a longer time and pierced more frequently on the artificial diet containing 2.0% gossypol, indicating that RNAi treated bugs reduced sensitivity to gossypol. Our findings suggest that AfasOBP11 may play a vital role in chemoreception of A. fasciaticollis, especially in gustatory perception.

Keywords: Adelphocoris fasciaticollis; AfasOBP11; EPG; Fluorescence binding assay; Gustatory perception; RNA interference; Sensilla on mouthparts.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Feeding Behavior
  • Female
  • Hemiptera / metabolism*
  • Hemiptera / ultrastructure
  • Male
  • Receptors, Odorant / metabolism*
  • Sensilla / metabolism*
  • Sensilla / ultrastructure
  • Taste*

Substances

  • Receptors, Odorant
  • odorant-binding protein