Laboratory of Functional Glycomics, College of Life Sciences, National Engineering Research Center for Miniaturized Detection System, Northwest University, Xi'an, People's Republic of China.
PLoS One. 2011;6(7):e22844. doi: 10.1371/journal.pone.0022844. Epub 2011 Jul 28.
Influenza virus typically alters protein glycosylation in order to escape immune pressure from hosts and hence to facilitate survival in different host environments. In this study, the patterns and conservation of glycosylation sites on HA and NA of influenza A/H1N1 viruses isolated from various hosts at different time periods were systematically analyzed, by employing a new strategy combining genome-based glycosylation site prediction and 3D modeling of glycoprotein structures, for elucidation of the modes and laws of glycosylation site alteration in the evolution of influenza A/H1N1 viruses. The results showed that influenza H1N1 viruses underwent different alterations of protein glycosylation in different hosts. Two alternative modes of glycosylation site alteration were involved in the evolution of human influenza virus: One was an increase in glycosylation site numbers, which mainly occurred with high frequency in the early stages of evolution. The other was a change in the positional conversion of the glycosylation sites, which was the dominating mode with relatively low frequency in the later evolutionary stages. The mechanisms and possibly biological functions of glycosylation site alteration for the evolution of influenza A/H1N1 viruses were also discussed. Importantly, the significant role of positional alteration of glycosylation sites in the host adaptation of influenza virus was elucidated. Although the results still need to be supported by experimental data, the information here may provide some constructive suggestions for research into the glycosylation of influenza viruses as well as even the design of surveillance and the production of viral vaccines.
流感病毒通常会改变蛋白质的糖基化，以逃避宿主的免疫压力，从而在不同的宿主环境中生存。在这项研究中，我们采用了一种新的策略，结合基于基因组的糖基化位点预测和糖蛋白结构的 3D 建模，系统地分析了不同时期从不同宿主中分离的甲型流感病毒（H1N1）HA 和 NA 上糖基化位点的模式和保守性，以阐明甲型流感病毒进化过程中糖基化位点改变的方式和规律。结果表明，流感 H1N1 病毒在不同宿主中经历了不同的蛋白质糖基化改变。人类流感病毒进化过程中涉及两种替代的糖基化位点改变模式：一种是糖基化位点数量的增加，这种情况主要发生在进化的早期阶段，频率较高。另一种是糖基化位点位置的转换，这种情况在进化后期以相对较低的频率为主导。还讨论了糖基化位点改变对甲型流感病毒进化的机制和可能的生物学功能。重要的是，阐明了糖基化位点位置改变在流感病毒宿主适应中的重要作用。尽管这些结果仍需要实验数据的支持，但这里的信息可能为流感病毒糖基化的研究甚至监测和病毒疫苗生产的设计提供一些建设性的建议。
