TAILIEUCHUNG - Báo cáo y học: " Antigenic analysis of classical swine fever virus E2 glycoprotein using pig antibodies identifies residues contributing to antigenic variation of the vaccine C-strain and group 2 strains circulating in China"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Antigenic analysis of classical swine fever virus E2 glycoprotein using pig antibodies identifies residues contributing to antigenic variation of the vaccine C-strain and group 2 strains circulating in China | Chen et al. Virology Journal 2010 7 378 http content 7 1 378 J VIROLOGY JOURNAL RESEARCH Open Access Antigenic analysis of classical swine fever virus E2 glycoprotein using pig antibodies identifies residues contributing to antigenic variation of the vaccine C-strain and group 2 strains circulating in China Ning Chen Chao Tong Dejiang Li Jing Wan Xuemei Yuan Xiaoliang Li Jinrong Peng Weihuan Fang Abstract Background Glycoprotein E2 the immunodominant protein of classical swine fever virus CSFV can induce neutralizing antibodies and confer protective immunity in pigs. Our previous phylogenetic analysis showed that subgroup viruses branched away from subgroup the vaccine C-strain lineage and became dominant in China. The E2 glycoproteins of CSFV C-strain and recent subgroup field isolates are genetically different. However it has not been clearly demonstrated how this diversity affects antigenicity of the protein. Results Antigenic variation of glycoprotein E2 was observed not only between CSFV vaccine C-strain and subgroup strains but also among strains of the same subgroup as determined by ELISA-based binding assay using pig antisera to the C-strain and a representative subgroup strain QZ-07 currently circulating in China. Antigenic incompatibility of E2 proteins markedly reduced neutralization efficiency against heterologous strains. Single amino acid substitutions of D705N L709P G713E N723S and S779A on C-strain recombinant E2 rE2 proteins significantly increased heterologous binding to anti-QZ-07 serum suggesting that these residues may be responsible for the antigenic variation between the C-strain and subgroup strains. Notably a G713E substitution caused the most dramatic enhancement of binding of the variant C-strain rE2 protein to anti-QZ-07 serum. Multiple sequence alignment revealed that the glutamic acid residue at this position is conserved within group 2 strains while the glycine residue is invariant among .

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