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目的分析近20年北半球甲型流感疫苗株血凝素(Hemagglutinin,HA)抗原的氨基酸和N-糖基化位点变异情况。方法利用生物信息学软件分析1990-2012年季节性流感疫苗株H1N1的4个抗原决定簇Sa、Sb、Ca、Cb和H3N2的4个抗原决定簇A、B、C、D的氨基酸和N-糖基化位点变异情况。结果 (1)H1N1疫苗株Sb抗原决定簇28、40位氨基酸N-糖基化位点相对保守,而142位氨基酸发生改变。(2)Sb抗原决定簇上无N-糖基化位点。(3)H3N2疫苗株B、D抗原决定簇2、479、181、301位氨基酸N-糖基化位点相对保守,而149位氨基酸发生改变。(4)H3N2疫苗株的N-糖基化位点不在抗原位点上。结论 (1)流感疫苗株HA抗原氨基酸变异集中在HA1蛋白环状部位。(2)流感疫苗株的N-糖基化位点在相对保守的序列,并且相同亚型的流感疫苗株有相似的N-糖基化位点。(3)HA蛋白变异可以推测流感病毒基因的改变,为选择与之匹配的流行株提供参考。
Objective To analyze the variation of amino acid and N-glycosylation sites of Hemagglutinin (HA) antigen in influenza A vaccine strains in the northern hemisphere in recent 20 years. Methods Bioinformatics software was used to analyze the amino acid residues A, B, C and D of four antigenic determinants Sa, Sb, Ca, Cb and H3N2 of seasonal influenza vaccine strain H1N1 from 1990 to 2012. The results showed that amino acids of N- Variation of glycosylation sites. Results (1) The amino acid N-glycosylation sites at amino acid positions 28 and 40 of the epitope of Sb antigen of H1N1 vaccine were relatively conservative while the amino acid at position 142 was changed. (2) There is no N-glycosylation site on the Sb antigenic determinant. (3) The amino acid N-glycosylation sites of amino acid residues 2,479,181,301 of B and D epitopes of H3N2 vaccine strain are relatively conservative while the amino acid at position 149 is changed. (4) The N-glycosylation site of H3N2 vaccine strain is not on the antigenic site. Conclusions (1) The amino acid variation of HA antigen in influenza vaccine strain is concentrated in the circular part of HA1 protein. (2) N-glycosylation sites of influenza vaccine strains are in a relatively conserved sequence, and influenza vaccine strains of the same subtype have similar N-glycosylation sites. (3) The variation of HA protein can predict the change of influenza virus gene and provide a reference for the selection of the matched epidemic strains.