Odorant ‐binding protein 19 in Monochamus alternatus involved in the recognition of a volatile strongly emitted from ovipositing host pines

OBP19 ofMonochamus alternatus is involved in detection of camphene, strongly emitted from ovipositing host. Double-stranded RNA producedvia transcription in vitro and bacteria-expressed system both lead to knockdown of OBP19. AbstractMonochamus alternatus is the primary carrier of pine wood nematodes, which pose a serious threat toPinus spp. in many countries. Newly emergingM. alternatus adults feed on heathy host pines, while matured adults transfer to stressed host pines for mating and oviposition. Several odorant-binding proteins (OBPs) ofM. alternatus have been proved to aid in the complex process of host location. To clarify the corresponding relations between OBPs and pine volatiles, more OBPs need to be studied. In this research, MaltOBP19 showed a specific expression in the antennae and mouthparts ofM. alternatus, and it was marked in 4 types of antenna sensilla by immunolocalization. Fluorescence binding assays demonstrated the high binding affinity of MaltOBP19 with camphene and myrcene in vitro. In Y-tube olfactory experiments,M. alternatus adults were attracted by camphene and RNAi of OBP19via microinjection significantly decreased their attraction index. Myrcene induced phobotaxis, but RNAi had no significant effect on this behavior. Further, we found that ingesting dsOBP19 produced by a bacteria-expressed system with a newly constructed vector could lead to the knockdown of MaltOBP19. These results suggest that MaltOBP19 may play a role in the process of host co...
Source: Insect Science - Category: Biology Authors: Tags: ORIGINAL ARTICLE Source Type: research
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