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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.