4.7 Article

Ligand-binding properties of odorant-binding protein 6 in Athetis lepigone to sex pheromones and maize volatiles

Journal

PEST MANAGEMENT SCIENCE
Volume 78, Issue 1, Pages 52-62

Publisher

JOHN WILEY & SONS LTD
DOI: 10.1002/ps.6606

Keywords

noctuid; odorant-binding protein; antennal-binding protein X; sex pheromone; maize; competitive binding assay; site-directed mutagenesis

Funding

  1. National Natural Science Foundation of China [31970456]
  2. Anhui Provincial Natural Science Foundation [2008085MC63]
  3. Natural Science Fund of Education Department of Anhui Province, China [KJ2019A0586]
  4. Overseas Visiting Program of Outstanding Young Talents Program of Anhui Province, China [gxgwfx2019023]
  5. Anhui College Students' Innovation and Entrepreneurship Training Program [202010373096, S202013620012]
  6. Youth Funding of Henan Academy of Agricultural sciences [2020YQ09]

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The olfactory function of Athetis lepigone is mediated by the odorant-binding protein AlepOBP6, which can recognize sex pheromones and maize volatiles. This protein may play a crucial role in mating, feeding, and oviposition behaviors, offering new insights into environmentally friendly pest management strategies.
BACKGROUND: Athetis lepigone, a noctuid moth feeding on more than 30 different crops worldwide, has evolved a sophisticated, sensitive, and specific chemosensory system to detect and discriminate exogenous chemicals. Odorant-binding proteins (OBPs) are the most important agent in insect chemosensory systems to be explored as an alternative target for environmentally friendly approaches to pest management. RESULTS: To investigate the olfactory function of A. lepigone OBPs (AlepOBPs), AlepOBP6 was identified and expressed in Escherichia coli. The binding affinity of the recombinant OBP to 20 different ligands was then examined using a competitive binding approach. The results revealed that AlepOBP6 can bind to two sex pheromones and ten maize volatiles, and its conformation stability is pH dependent. We also carried out a structure-function study using different molecular approaches, including structure modeling, molecular docking, and a mutation functional assay to identify amino acid residues (M39, V68, W106, Q107, and Y114) involved in the binding of AlepOBP6 to both sex pheromones and maize volatiles in A. lepigone. CONCLUSION: These results suggest that AlepOBP6 is likely involved in mediating the responses of A. lepigone to sex pheromones and maize volatiles, which may play a pivotal function in mating, feeding, and oviposition behaviors. This study not only provides new insight into the binding mechanism of OBPs to sex pheromones and host volatiles in moths, but also contributes to the discovery of novel target candidates for developing efficient behavior disruptors to control A. lepigone in the future.

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