Bioinformatics Analysis of the VP2 Protein of GII.4 Norovirus
Article
Figures
Metrics
Preview PDF
Reference
Related
Cited by
Materials
Abstract:
In order to understand the biological characteristics of the VP2 protein of norovirus (NoV), the VP2 protein of current NoV epidemic strains was used as the research object in this study. Bioinformatics softwares were used to predict and analyze the physico-chemical properties, phosphorylation sites, glycosylation sites, transmembrane regions, signal peptides, secondary structures, tertiary structure, antigenic determinants and B cell epitopes of NoV VP2 protein. The results showed that the VP2 protein of epidemic NoV strain was a stable hydrophilic protein with an average isoelectric point of 10.47, a water absorption coefficient of -0.47, and an instability coefficient of 47.91, with basic amino acids accounting for about 11.60%. The VP2 protein contains about 43 potential phosphorylation modification sites and 2 potential glycosylation modification sites. Most strains do not contain transmembrane domains and signal peptides, however, the GI.3 VP2 protein has the transmembrane domain and signal peptide. The average proportion of α-helix, extended chain, β-fold and irregular coil were 38.17%, 7.45%, 6.25% and 48.13%, respectively. The protein coverage of the tertiary structure prediction model was 56.70%. There were 8 potential protein antigenic determinants and 25 B cell epitopes on average. In this study, bioinformatics analysis methods were used to predict the physicochemical properties and structures of the VP2 protein of the currently epidemic NoV GII.4 strains, which has laid a theoretical foundation for further research on the function of the NoV VP2 protein.
