In silico analysis of the interaction of Syntaxin-18, a putative receptor of Peregrinus maidis (Ashmead) (Hemiptera: Delphacidae) with Maize mosaic virus glycoprotein

Abstract

The corn planthopper, Peregrinus maidis, is a widely distributed insect pest which serve as vector of two plant pathogenic viruses, Maize mosaic virus (MMV) and Maize stripe virus (MStV). It transmits the viruses in a persistent, circulative, and propagative manner. MMV is an alphanucleorhabdovirus with a negative-sense, single-stranded (ss) RNA unsegmented genome. Previous work using the membrane-based yeast two hybrid system on this pathosystem identified potential receptors for MMV. One identified insect vector protein is Syntaxin-18 (PmSTX18) which belongs to the SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) family of proteins. SNAREs play major roles in the final stage of the docking and the subsequent fusion of diverse vesicle-mediated transport events. In this work, in silico analysis of the interaction of MMV glycoprotein (MMV G) and PmSTX18 was performed. Functional annotation of PmSTX18 and MMV G was done to develop a reliable model for PmSTX18—MMV G interaction. Analysis and protein-protein interaction (PPI) prediction used sequence-based and structure-based approaches. Results showed that the four best predicted docked complexes have 45, 42, 22 and 27 amino acid interacting residues with binding affinities (change in Gibbs free energy, ΔG) of -57.73, -57.05, -52.55, and -51.69, respectively, suggesting strong interactions. This is the first in silico analysis performed for the interaction on a putative receptor of P. maidis and MMV G. The results of the PPI prediction provide novel information for studying the role of STX18 in the transport, docking and fusion events of the virus in the insect vector host.