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- W2361491551 abstract "Objective To use bioinformatics to analyze the structure and predict the B-cell-epitopes of the protein Sao in order to screen sequences to design a vaccine against Streptococcus suis type 2. Methods Based on the sequence of the Sao protein,the basic physical and chemical properties,transmembrane domains,secondary structures,tertiary structure,hydrophilicity,flexibility,surface accessibility,and antigen epitopes of the protein Sao were predicted using bioinformatics software. Results Results indicated that the carboxy-terminal of the protein Sao had seven highly conserved repeats and one LPVTG membrane anchor motif.The random coil accounted for 74.21%of the protein,and simulation of the three-dimensional conformation was consistent with the predicted secondary structure.The hydrophilic region accounted for 76.21% of the protein,the flexible region accounted for 64.06%,and the region with an accessible surface accounted for 75.04%.Sao had multiple linear epitopes and two protein sequences had potential for design of a vaccine.BLAST results showed that these two sequences only existed in S.suis and were highly conserved in the pathogenic S.suis serotypes 1,2,1/2,3,7,9,and 14. Conclusion Sao is an unstable protein with strong hydrophilicity.The two screened protein sequence were highly conserved and had strong antigenicity and could be used to genetically engineer a vaccine." @default.
- W2361491551 created "2016-06-24" @default.
- W2361491551 creator A5018244700 @default.
- W2361491551 date "2014-01-01" @default.
- W2361491551 modified "2023-09-23" @default.
- W2361491551 title "Bioinformatics analysis of Sao protein and design of a vaccine against Streptococcus suis type 2" @default.
- W2361491551 hasPublicationYear "2014" @default.
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