摘要
目的:从分子进化水平上分析流感的起源及发展问题,研究目前爆发的H1N1病毒的HA分子的变异行为。方法:以GenBank公布的甲型流感H1N1病毒血凝素(hemagglutinin,HA)核酸序列和我国及世界范围内近几年来报告的H1N1流感病毒HA的核酸及氨基酸序列为研究对象,利用CLUSTAL1.83和NetNGlyc1.0等生物信息学软件对HA核酸和氨基酸序列进行了比对分析;将其糖基化位点、氨基酸序列和抗原决定簇与以往流感病毒进行了比较。同时,还将人源和猪源甲型H1N1流感病毒的HA氨基酸序列进行了序列比对和系统发育分析。结果:最新爆发的甲型H1N1流感病毒的HA除了在60,259,453,512位点高度保守区域与之前爆发的流感病毒一致外,在249位点新出现1个"-NTT-"的糖基化位点。发现所有的甲型病毒的氨基酸序列在8个氨基酸位点均发生改变,而8个氨基酸位点位于6个抗原抗原决定簇上。结论:糖基化位点的增加,氨基酸位点的改变导致抗原决定簇的改变,即抗原性漂移现象,都成为引起其传染性改变的重要原因。
Objective: To investigate the genesis and development of influenza in molecule level, and to investigate the vanauon of Influenza HA in H1N1. Method: The nucleotide sequences of the new public and recent few years' influenza A H1N1 virus' hemagglutinin (HA) from all over the world were used as analysis objects in this research. The HA's glycosylation site, antigen determinant sites, amino acid sequences were analyze by bioinformatics software-CLUSTAL 1.83 and NetNGlyc 1.0 edc. The results reveal that there is high conservation area in HA of H1N1 between the recent influenza and the previous influenza. At last, the origin of influenza from the cladogram and verificate the some theory about resource were analyzed. Result: There is a new glycosylation site "-NTT-"in the position 249. Compared with the sequences of the human resource and the swine resource, there are 8 amino acid sites changed, which present in 6 antigen determinant sites. Conclusion: The increase of the glycosylation site, the change of amino acid sites lead to the change of the antigen determinant sites,the antigenic drift phenomenon which all could be the reason of transmissibility change.
出处
《现代生物医学进展》
CAS
2009年第20期3801-3806,共6页
Progress in Modern Biomedicine