本文選題：HN甲型流感病毒 + 血凝素蛋白��； 參考：《南昌大學(xué)學(xué)報(bào)(醫(yī)學(xué)版)》2016年05期

【摘要】：目的比較2007—2014年分離的H1N1甲型流感病毒H1血凝素蛋白與分離于1934年的H1N1甲型流感病毒H1血凝素蛋白的差異性,以了解近幾年流行的H1N1甲型流感病毒H1血凝素蛋白的變異特征。方法從Genebank的基因數(shù)據(jù)庫中獲取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,采用在線軟件SignalP4.1預(yù)測信號(hào)肽,運(yùn)用Clustal X,Bioedit等國際通用軟件進(jìn)行氨基酸和核苷酸的序列比對(duì),計(jì)算核苷酸及氨基酸的同源性。在線軟件Antheprot分析二級(jí)結(jié)構(gòu)。結(jié)果 H1血凝素蛋白編碼框架長約1701bp,編碼含566個(gè)氨基酸組成的多肽。16株H1N1甲型流感病毒H1血凝素氨基酸同源性為92.4%~99.8%,核苷酸同源性為91.8%~99.6%。H1血凝素蛋白aa1-aa17區(qū)域?yàn)闈撛谛盘?hào)肽,血凝素蛋白A1和A2裂解序列為位于aa324-aa330序列IQSR↓GLF。H1血凝素蛋白富含潛在α螺旋(25%~32%)、β折疊(27%~28%)和卷曲結(jié)構(gòu)(23%~26%)等二級(jí)結(jié)構(gòu)。2007—2014年的15株病毒的血凝素蛋白A1高變區(qū)位于羧基端aa278-aa321,有11個(gè)位點(diǎn)變異,變異率高達(dá)25%。參與二硫鍵形成的10個(gè)半胱氨酸位點(diǎn)未發(fā)生變異,3個(gè)受體結(jié)合區(qū)的氨基酸序列(PKTS、VLVLWAIHH和SRYSKKFK)比較保守,有2個(gè)序列出現(xiàn)毒力相關(guān)位點(diǎn)D222G突變。結(jié)論與1934年的H1N1甲型流感病毒H1血凝素蛋白比較,2007—2014年間分離H1N1甲型流感病毒H1血凝素蛋白的重要功能結(jié)構(gòu)域的序列仍保守穩(wěn)定,但在某些位點(diǎn)出現(xiàn)較高頻率的替代變異。
[Abstract]:Objective to compare the difference of H1 hemagglutinin protein of H1N1 influenza A virus and H1N1 influenza A virus H1 hemagglutinin protein isolated from 2007 to 2014 in order to understand the variation of H1 hemagglutinin protein of H1N1 influenza A virus in recent years. Methods the nucleotide and amino acid sequences of H1 hemagglutinin protein of H1N1 influenza A virus were obtained from Genebank gene database. The signal peptide was predicted by online software SignalP4.1. The sequence alignment of amino acids and nucleotides was carried out by using Clustal XG Bioedit and other international software, and the homology of nucleotides and amino acids was calculated. The secondary structure is analyzed by online software Antheprot. Results the coding frame of H1 hemagglutinin protein was about 1701 BP, encoding 566 amino acids. The amino acid homology of H1 hemagglutinin encoding H1N1 influenza A virus H1 hemagglutinin was 92.4% and 99.8, and the nucleotide homology was 91.8%~99.6%.H1 hemagglutinin protein aa1-aa17 region, which was potential signal peptide. Hemagglutinin A 1 and A 2 cleavage sequences are located in the secondary structure of aa324-aa330 sequence IQSR IQSR GLF.H1 hemagglutinin protein rich in potential 偽 helix 2532T, 尾 folding 2728T) and crimp structure 23x2626.The high variation region of hemagglutinin A1 of 15 strains of virus from 2007 to 2014 is located in carboxylic acid. The base terminal aa278-aa321 has 11 loci. The mutation rate is as high as 25. The 10 cysteine sites involved in the formation of disulfide bonds were not mutated, and the amino acid sequences of the three receptor binding regions, PKTS VLVLWAIHH and SRYSKKFK, were conserved, and two of them showed D222G mutations in virulence related sites. Conclusion compared with the H1 hemagglutinin protein of H1N1 influenza A virus in 1934, the sequence of important functional domain of H1 hemagglutinin protein isolated from H1N1 A influenza virus from 2007 to 2014 is still conserved and stable, but there is a high frequency of substitution variation at some sites.
【作者單位】： 南昌大學(xué)公共衛(wèi)生學(xué)院;南昌大學(xué)撫州醫(yī)學(xué)院;南昌大學(xué)基礎(chǔ)醫(yī)學(xué)院微生物學(xué)教研室;
【分類號(hào)】：R373.13

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