Abstract:

[Objective] The aim of this study was to conduct bioinformatics analysis on the pS273R protein of African swine fever virus （ASFV）. [Method] Using bioinformatics tools, the sequence homology and genetic evolution of the pS273R gene of 43 strains of ASFV were analyzed, and predictions were made on the physicochemical properties, secondary structure, phosphorylation sites, glycosylation modifications, subcellular localization and tertiary structure of the pS273R protein. [Result] Different ASFV strains exhibited high homology in pS273R gene with 5 strains isolated from China sharing 100% sequence homology, and 38 strains isolated from other countries sharing 93.60% to 100% sequence homology. Phylogenetic analysis showed that the Chinese strains were genetically closely related to the European branch. The pS273R protein was hydrophilic and composed of 273 amino acids, with a predicted molecular weigh of 31.58 kDa. In terms of secondary structure, α-helix （Hh）, extended chain （Ee）, β-bend （Tt） and random coil （Cc） were mainly observed. It had 28 phosphorylation sites and 2 potential N-glycosylation sites. It most likely presented in the cytoplasm of the host cell （P=47.8%）. The tertiary structure was formed through biological processes such as rotation, folding and curling of the secondary structure of α-helix, β-bend, β-fold and random coil. [Conclusion] The results obtained in this study provide references for the in-depth analysis of structure and function of pS273R protein and the development of ASFV inhibitors.

Key words: African swine fever virus, pS273R protein, bioinformatics analysis