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Molecular characterization and functional analysis of pheromone binding protein 1 from Cydia pomonella (L.)
Author(s) -
Tian Z.,
Zhang Y.
Publication year - 2016
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.12261
Subject(s) - biology , pheromone , botany , computational biology
A full‐length cDNA encoding Cydia pomonella pheromone binding protein 1 (CpomPBP1) was cloned and characterized. CpomPBP1, possessing the typical characteristics of lepidopteran odorant binding proteins, was detected to be specifically expressed in the antennae of male and female moths at the mRNA and protein level. Soluble recombinant CpomPBP1 was subjected to in vitro binding to analyse its binding properties and to search for potentially active semiochemicals. A competitive binding assay showed that three 12‐carbon ligands, codlemone, 1‐dodecanol and E,E‐2,4‐dodecadienal, were able to bind to CpomPBP1 in decreasing order of affinity. Moreover, unlike the wild‐type CpomPBP1, the C‐terminus truncated CpomPBP1 exhibited high affinity to ligands even in an acidic environment, suggesting that the C‐terminus plays a role in preventing ligands from binding to CpomPBP1 in a lower pH environment.