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目的比较2007—2014年分离的H1N1甲型流感病毒H1血凝素蛋白与分离于1934年的H1N1甲型流感病毒H1血凝素蛋白的差异性,以了解近几年流行的H1N1甲型流感病毒H1血凝素蛋白的变异特征。方法从Genebank的基因数据库中获取16株H1N1甲型流感病毒H1血凝素蛋白的核苷酸和氨基酸序列,采用在线软件SignalP4.1预测信号肽,运用Clustal X,Bioedit等国际通用软件进行氨基酸和核苷酸的序列比对,计算核苷酸及氨基酸的同源性。在线软件Antheprot分析二级结构。结果 H1血凝素蛋白编码框架长约1701bp,编码含566个氨基酸组成的多肽。16株H1N1甲型流感病毒H1血凝素氨基酸同源性为92.4%~99.8%,核苷酸同源性为91.8%~99.6%。H1血凝素蛋白aa1-aa17区域为潜在信号肽,血凝素蛋白A1和A2裂解序列为位于aa324-aa330序列IQSR↓GLF。H1血凝素蛋白富含潜在α螺旋(25%~32%)、β折叠(27%~28%)和卷曲结构(23%~26%)等二级结构。2007—2014年的15株病毒的血凝素蛋白A1高变区位于羧基端aa278-aa321,有11个位点变异,变异率高达25%。参与二硫键形成的10个半胱氨酸位点未发生变异,3个受体结合区的氨基酸序列(PKTS、VLVLWAIHH和SRYSKKFK)比较保守,有2个序列出现毒力相关位点D222G突变。结论与1934年的H1N1甲型流感病毒H1血凝素蛋白比较,2007—2014年间分离H1N1甲型流感病毒H1血凝素蛋白的重要功能结构域的序列仍保守稳定,但在某些位点出现较高频率的替代变异。
Objective To compare the difference between the H1N1 influenza virus H1 hemagglutinin protein isolated in 2007-2014 and the H1N1 influenza virus H1 hemagglutinin protein isolated in 1934 in order to understand the prevalence of H1N1 influenza A virus in recent years H1 hemagglutinin protein variation characteristics. Methods The nucleotide and amino acid sequences of 16 H1N1 influenza virus H1 hemagglutinin proteins were obtained from the Genebank database. The signal peptides were predicted by online software SignalP4.1. The amino acids and amino acids Nucleotide sequence alignment, calculation of nucleotide and amino acid homology. Online software Antheprot analyzes secondary structure. Results The H1 hemagglutinin coding sequence was about 1701 bp in size and encoded a polypeptide of 566 amino acids. The homologies of the H1 hemagglutinin of the 16 H1N1 influenza A viruses ranged from 92.4% to 99.8% with nucleotide homology of 91.8% to 99.6%. H1 hemagglutinin aa1-aa17 region is a potential signal peptide, hemagglutinin A1 and A2 cleavage sequence is located in the aa324-aa330 sequence IQSR ↓ GLF. H1 hemagglutinin is enriched in secondary structures such as potential α helix (25% -32%), β-sheet (27% -28%) and curly structure (23% -26%). The hemagglutinin A1 hypervariable region of 15 viruses from 2007 to 2014 was located at the carboxy terminal aa278-aa321, with 11 loci variation with mutation rate as high as 25%. The ten cysteine sites involved in disulfide bond formation were not mutated. The amino acid sequences of the three receptor binding regions (PKTS, VLVLWAIHH and SRYSKKFK) were relatively conservative. Two of the sequences showed the D222G mutation in virulence-related sites. Conclusion Compared with the H1N1 H1N1 hemagglutinin protein of 1934, the sequence of the important functional domains of the H1N1 H1 hemagglutinin protein isolated from 2007 to 2014 is still conservative, but some sites appear Alternate mutation at higher frequencies.