Glycosylation and an amino acid insertion in the head of hemagglutinin independently affect the antigenic properties of H5N1 avian influenza viruses
Glycosylation and an amino acid insertion in the head of hemagglutinin independently affect the antigenic properties of H5N1 avian influenza viruses
复制标题
血凝素头部的糖基化和氨基酸插入独立影响 H5N1 禽流感病毒的抗原特性
DOI：
10.1007/s11427-018-9439-0
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发表时间：
2019-01-01
影响因子：
9.1
通讯作者：
Chen, Hualan
中科院分区：
文献类型：
--
作者：
Gu, Chunyang;Zeng, Xianying;Chen, Hualan
抗原漂移迫使我们经常更新流感疫苗；然而，抗原变异的遗传基础在很大程度上仍不清楚。在本研究中，我们以分支7.2 H5病毒为模型，探讨流感病毒抗原变异的分子决定因素。我们制备了8株针对指标病毒A/FICE/山西/2/2006的血凝素(HA)蛋白的单抗，发现两株具有代表性的抗原漂移的分支7.2病毒与8株单抗中的6株不发生反应。E131N突变和抗原漂移株HA蛋白134位亮氨酸的插入消除了病毒与单抗的反应性。我们还发现H5 HA蛋白中的氨基酸N131是糖基化的。我们的结果提供了糖基化和HA中的氨基酸插入或缺失影响抗原变异的实验证据。
Antigenic drift forces us to frequently update influenza vaccines; however, the genetic basis for antigenic variation remains largely unknown. In this study, we used clade 7.2 H5 viruses as models to explore the molecular determinants of influenza virus antigenic variation. We generated eight monoclonal antibodies (MAbs) targeted to the hemagglutinin (HA) protein of the index virus A/chicken/Shanxi/2/2006 and found that two representative antigenically drifted clade 7.2 viruses did not react with six of the eight MAbs. The E131N mutation and insertion of leucine at position 134 in the HA protein of the antigenically drifted strains eliminated the reactivity of the virus with the MAbs. We also found that the amino acid N131 in the H5 HA protein is glycosylated. Our results provide experimental evidence that glycosylation and an amino acid insertion or deletion in HA influence antigenic variation.