The evolutionary pattern of glycosylation sites in influenza virus (H5N1) hemagglutinin and neuraminidase.
The evolutionary pattern of glycosylation sites in influenza virus (H5N1) hemagglutinin and neuraminidase.
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DOI：
10.1371/journal.pone.0049224
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发表时间：
2012
期刊：
影响因子：
3.7
通讯作者：
Li Z
中科院分区：
文献类型：
--
作者：
Chen W;Zhong Y;Qin Y;Sun S;Li Z
流感病毒表面的两种糖蛋白血凝素（HA）和神经氨酸酶（NA）在跨区系、膜融合和子代病毒体释放中起着关键作用。为了探索这两种糖蛋白中N-糖基化位点（糖位点）的分布，我们收集并比对了所有HA和NA亚型的氨基酸序列。两个糖基位于HA 0切割位点和融合肽，并在所有HA亚型中惊人地保守，而其余的糖基是其亚型所特有的。在NA的茎域中发现了2 ~ 4个保守的糖基，但这些糖基会受到特定茎域序列缺失的影响。另一个高度保守的糖基出现在四聚体全局结构域的顶部中心，而其他糖基则分布在全局结构域的周围。在这里，我们提出了一个详细的调查，在IV的包膜糖蛋白的糖位点的分布和进化模式，并进一步集中在H5 N1病毒，并得出结论，在H5 N1的糖位点变得更加复杂，在HA和NA的影响在过去的五年。
Two glycoproteins, hemagglutinin (HA) and neuraminidase (NA), on the surface of influenza viruses play crucial roles in transfaunation, membrane fusion and the release of progeny virions. To explore the distribution of N-glycosylation sites (glycosites) in these two glycoproteins, we collected and aligned the amino acid sequences of all the HA and NA subtypes. Two glycosites were located at HA0 cleavage sites and fusion peptides and were strikingly conserved in all HA subtypes, while the remaining glycosites were unique to their subtypes. Two to four conserved glycosites were found in the stalk domain of NA, but these are affected by the deletion of specific stalk domain sequences. Another highly conserved glycosite appeared at the top center of tetrameric global domain, while the others glycosites were distributed around the global domain. Here we present a detailed investigation of the distribution and the evolutionary pattern of the glycosites in the envelope glycoproteins of IVs, and further focus on the H5N1 virus and conclude that the glycosites in H5N1 have become more complicated in HA and less influential in NA in the last five years.
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影响因子：
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作者：
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