Glycosylation at Asn91 of H1N1 haemagglutinin affects binding to glycan receptors.
Glycosylation at Asn91 of H1N1 haemagglutinin affects binding to glycan receptors.
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DOI：
10.1042/bj20112101
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发表时间：
2012-06-15
期刊：
影响因子：
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通讯作者：
Sasisekharan R
中科院分区：
文献类型：
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作者：
Jayaraman A;Koh X;Li J;Raman R;Viswanathan K;Shriver Z;Sasisekharan R
甲型流感病毒表面上的糖蛋白HA（血凝素）在识别和结合特异性宿主细胞表面聚糖受体以及在病毒复制期间病毒膜与宿主核膜的融合中起核心作用。鉴于病毒表面上HA的丰度，这种蛋白质也是宿主先天性和适应性免疫应答的主要靶标。尽管HA上糖基化位点的添加是病毒进化的一部分以逃避宿主免疫应答，但在病毒的大部分进化过程中存在保守的特异性糖基化位点。在本研究中，证明了H1N1 HA中Asn91处的一个这样的保守糖基化位点决定性地控制聚糖受体结合特异性，因此可能会影响病毒的宿主适应性。
The glycoprotein HA (haemagglutinin) on the surface of influenza A virus plays a central role in recognition and binding to specific host cell-surface glycan receptors and in fusion of viral membrane to the host nuclear membrane during viral replication. Given the abundance of HA on the viral surface, this protein is also the primary target for host innate and adaptive immune responses. Although addition of glycosylation sites on HA are a part of viral evolution to evade the host immune responses, there are specific glycosylation sites that are conserved during most of the evolution of the virus. In the present study, it was demonstrated that one such conserved glycosylation site at Asn91 in H1N1 HA critically governs the glycan receptor-binding specificity and hence would potentially impinge on the host adaptation of the virus.