SAFETYLIT WEEKLY UPDATE

We compile citations and summaries of about 400 new articles every week.
RSS Feed

HELP: Tutorials | FAQ
CONTACT US: Contact info

Search Results

Journal Article

Citation

Wang L, Zhu JY, Qian C, Fang Q, Ye GY. Arch. Insect Biochem. Physiol. 2014; 88(2): 101-110.

Affiliation

College of Life Science, Anhui Agricultural University, Hefei, China; State Key Laboratory of Rice Biology, Ministry of Agriculture Key Laboratory of Agricultural Entomology, Institute of Insect Sciences, Zhejiang University, Hangzhou, China.

Copyright

(Copyright © 2014, John Wiley and Sons)

DOI

10.1002/arch.21206

PMID

25256903

Abstract

Odorant binding proteins (OBPs) are crucial for insects to detect food, mates, predators, or other purposes. They are mostly located on antennae and other olfactory sensilla. In this study, we identified an OBP from the venom of Pteromalus puparum, designated as PpOBP. The cDNA of PpOBP is 517 bp in length, encoding 132 amino acids. Phylogenetic analysis revealed that PpOBP was clustered with OBP68 and OBP67 of Nasonia vitripennis. PpOBP was highly expressed in the venom apparatus at the transcriptional and translational levels. PpOBP was located in all parts of venom apparatus including venom gland, venom reservoir, and Dufour's gland. During 0-6 days post adult eclosion, the PpOBP mRNA level peaked at 2 days in the venom apparatus, whereas the protein remained at a high level. In the venom apparatus, the PpOBP mRNA was significantly upregulated following feeding with honey and parasitization. We propose that PpOBP is involved in parasitoid-host interactions.


Language: en

NEW SEARCH


All SafetyLit records are available for automatic download to Zotero & Mendeley
Print