In silico structure-based analysis of the predicted protein-protein 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 serves as a vector of two phytopathogenic viruses, Maize mosaic virus (MMV) and Maize stripe virus (MStV). It transmits the viruses in a persistent and propagative manner. MMV is an alphanucleorhabdovirus with a negative-sense, single-stranded (ss) RNA unsegmented genome. One identified insect vector protein that may serve as receptor to MMV is Syntaxin-18 (PmStx18) which belongs to the SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors). SNAREs play major roles in the final stage of docking and 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. Various freely available protein-protein docking web servers were used to predict the 3D complex of MMV G and PmStx18. Analysis and protein-protein interaction (PPI) count showed that the complex predicted by the ZDOCK server has the highest number of interaction and highest affinity, as suggested by the calculated solvation free energy gain upon formation of the interface (ΔiG = −31 kcal/mol). Molecular dynamics simulation of the complex revealed important interactions at the interface over the course of 50 ns. 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 protein-protein interaction prediction provide novel information for studying the role of STX18 in the transport, docking and fusion events involved in virus particle transport in the insect vector cells and its release.
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