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Arch Insect Biochem Physiol

Title:		"Structural investigation of selective binding dynamics for the pheromone-binding protein 1 of the grapevine moth, Lobesia botrana"
Author(s):		Venthur H; Machuca J; Godoy R; Palma-Millanao R; Zhou JJ; Larama G; Bardehle L; Quiroz A; Ceballos R; Mutis A;
Address:		"Laboratorio de Quimica Ecologica, Departamento de Ciencias Quimicas y Recursos Naturales, Universidad de La Frontera, Temuco, Chile. Centro de Investigacion Biotecnologica Aplicada al Medio Ambiente, CIBAMA, Universidad de La Frontera, Temuco, Chile. Departamento de Ciencias Quimicas y Recursos Naturales, Carrera Bioquimica, Universidad de La Frontera, Temuco, Chile. Millenium Nucleus Centre in Molecular Ecology and Evolutionary Applications in Agroecosystems, Instituto de Ciencias Biologicas, Universidad de Talca, Talca, Chile. Department of Biological Chemistry and Crop Protection, Rothamsted Research, Herts, United Kingdom. Jilin Provincial Key Laboratory of Animal Resource Conservation and Utilization, Northeast Normal University, Changchun, China. Departamento de Ingenieria Matematica, Universidad de La Frontera, Temuco, Chile. Centro de Excelencia de Modelacion y Computacion Cientifica, Universidad de La Frontera, Temuco, Chile. Laboratorio de Ecologia Quimica, Centro Tecnologico de Control Biologico, Instituto de Investigaciones Agropecuarias (INIA)-Quilamapu, Chillan, Chile"
Journal Title:		Arch Insect Biochem Physiol
Year:		2019
Volume:		20190507
Issue:		3
Page Number:		e21557 -
DOI:		10.1002/arch.21557
ISSN/ISBN:		1520-6327 (Electronic) 0739-4462 (Linking)
Abstract:		"The European grapevine moth, Lobesia botrana (Denis & Schiffermuller), is a serious pest in vineyards in North and South America. Mating disruption techniques have been used to control and monitor L. botrana on the basis of its sexual communication. This needs a well-tuned olfactory system, in which it is believed that pheromone-binding proteins (PBPs) are key players that transport pheromones in the antennae of moths. In this study, the selectivity of a PBP, named as LbotPBP1, was tested by fluorescence binding assays against 11 sex pheromone components and 6 host plant volatiles. In addition, its binding mechanism was predicted on the basis of structural analyses by molecular docking and complex and steered molecular dynamics (SMD). Our results indicate that LbotPBP1 binds selectively to sex pheromone components over certain host plant volatiles, according to both in vitro and in silico tests. Thus, chain length (14 carbon atoms) and functional groups (i.e., alcohol and ester) appear to be key features for stable binding. Likewise, residues such as Phe12, Phe36, and Phe118 could participate in unspecific binding processes, whilst Ser9, Ser56, and Trp114 could participate in the specific recognition and stabilization of sex pheromones instead of host plant volatiles. Moreover, our SMD approach supported 11-dodecenyl acetate as the best ligand for LbotPBP1. Overall, the dynamics simulations, contact frequency analysis and SMD shed light on the binding mechanism of LbotPBP1 and could overcome the imprecision of molecular docking, supporting the in vitro binding assays. Finally, the role of LbotPBP1 in the chemical ecology of L. botrana is discussed"
Keywords:		Animals Carrier Proteins/*genetics/metabolism Insect Proteins/*genetics/metabolism Male Molecular Docking Simulation Moths/*genetics/metabolism Protein Binding Sex Attractants/*metabolism Tortricidae molecular modeling odorant-binding protein olfactory sy;
Notes:		"MedlineVenthur, Herbert Machuca, Juan Godoy, Ricardo Palma-Millanao, Ruben Zhou, Jing-Jiang Larama, Giovanni Bardehle, Leonardo Quiroz, Andres Ceballos, Ricardo Mutis, Ana eng DI18-1002/Universidad de La Frontera/ 11140668/Fondo Nacional de Desarrollo Cientifico y Tecnologico/ 2019/05/08 Arch Insect Biochem Physiol. 2019 Jul; 101(3):e21557. doi: 10.1002/arch.21557. Epub 2019 May 7"