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In silico analyses of molecular interactions between groundnut bud necrosis virus and its vector, Thrips palmi

Jagdale, Shounak S., Ghosh, Amalendu
Virusdisease 2019 v.30 no.2 pp. 245-251
phosphopyruvate hydratase, tomatoes, Thrips palmi, virion, H-transporting ATP synthase, H+/K+-exchanging ATPase, genome, lectins, Groundnut bud necrosis tospovirus, vacuoles, endocytosis, amino acids, signal peptide, clathrin, cathepsins, glycoproteins
Groundnut bud necrosis virus (GBNV) is an economically important tospovirus transmitted by Thrips palmi (Thysanoptera: Thripidae). The current understanding of thrips-tospovirus interactions is largely based on the tomato spotted wilt virus-Frankliniella occidentalis relationship. Only limited information is available for the GBNV-T. palmi system. In the present study, available genome data of T. palmi and GBNV were used to predict the protein partners that may play a crucial role in the internalization of GBNV virions into thrips cells. Computational analyses showed that the GBNV precursor glycoprotein bears a signal peptide of 24 amino acids and a secondary cleavage site at position 434–435 separates the amino-terminal mature glycoprotein (GN) from the carboxyl-terminal glycoprotein (GC). Potential interactions of GBNV glycoproteins were predicted with T. palmi enolase, cathepsin, C-type lectin, clathrin and vacuolar ATP synthase subunit E. The in silico analyses suggested that C-type lectin is the primary cellular receptor to interact with GBNV-GN. After receptor binding, virus particles probably enter vector cells by clathrin-mediated endocytosis. This is the first in silico evidence of GBNV-T. palmi protein interaction.