Identification of pheromone-binding proteins of the maize stem borer, Chilo partellus (Swinhoe, 1885) (Lepidoptera: Crambidae)

Abstract

Pheromone-binding proteins (PBPs) play a significant role in olfaction and mating. The present work was designed to isolate, extract, and purify the pheromone-binding proteins from the antennae of male Chilo partellus (Swinhoe, 1885) (Lepidoptera: Crambidae). The pheromone-binding proteins extracted from the male antennae were found to be 770 μg in 100 mg of sample. Pheromone-binding protein molecular weight was determined as 17 kDa by SDS-PAGE analysis. Identified proteins were purified through gel extraction with a recovery percentage of proteins up to 95%. Purified protein samples are analyzed on native PAGE gels. Relative mobility of proteins was determined as 0.574 nm in the densitometry analysis. These identified pheromone-binding proteins can be used for identification of novel pheromone compounds in in vitro studies. This study can be helpful in designing integrated pest management programs to control the maize stem borer by mass trapping of male moths.

Sex-specific spatial and temporal gene expressions of Pheromone biosynthesis activating neuropeptide (PBAN) and binding proteins (PBP/OBP) in Spoladea recurvalis

“…Some studies have suggested that dendrites that adjoining to the soluble PBPs/OBP in sensillum lymph were anticipated to relocate the dendrite membrane of the sensory neurons from the hydrophobic pheromone 22 . Other studies reported that PBPs attributed to certain receptions of sex-pheromone components, although PBPs were capable of binding to numerous pheromone components 22,25,53–55 . This was because of the fact that the complex peripheral mechanism in the olfactory system possesses the ability to purify the selection.…”