Bat-Derived Influenza Hemagglutinin H17 Does Not Bind Canonical Avian or Human Receptors and Most Likely Uses a Unique Entry Mechanism
Bat-Derived Influenza Hemagglutinin H17 Does Not Bind Canonical Avian or Human Receptors and Most Likely Uses a Unique Entry Mechanism
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DOI：
10.1016/j.celrep.2013.01.025
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发表时间：
2013-03-01
期刊：
影响因子：
8.8
通讯作者：
Gao, George F.
中科院分区：
文献类型：
--
作者：
Sun, Xiaoman;Shi, Yi;Gao, George F.
最近在蝙蝠中发现了一种新的流感样病毒基因组（H17N10），为流感病毒的起源和进化提供了新的视角。病毒包膜糖蛋白血凝素（HA）负责流感病毒受体的结合、融合和进入细胞；因此，对HA H17的结构和功能进行了表征。2.70埃分辨率的晶体结构显示H17具有典型的甲型流感病毒HA折叠，但具有一些特殊特征，包括假设唾液酸（SA）结合位点扭曲和低热稳定性。未观察到与典型的人α 2,6 sa -连锁或禽α 2,3 sa -连锁受体结合。此外，使用覆盖600多个聚糖的芯片未检测到H17聚糖的结合。我们的研究结果表明，H17在特征HAs中是独特的，并且与典型流感病毒相比，蝙蝠衍生的流感病毒可能使用不同的进入机制。
A new influenza-like virus genome (H17N10) was recently discovered in bats and offers a new perspective about the origin and evolution of influenza viruses. The viral envelope glycoprotein hemagglutinin (HA) is responsible for influenza virus receptor binding, fusion, and entry into the cell; therefore, the structure and function of HA H17 was characterized. The 2.70 angstrom resolution crystal structure revealed that H17 has a typical influenza A virus HA fold, but with some special features, including a distorted putative sialic acid (SA) binding site and low thermostability. No binding to either the canonical human alpha 2,6 SA-linkage or avian alpha 2,3 SA-linkage receptor was observed. Furthermore, H17 glycan binding was not detected using a chip covering more than 600 glycans. Our results demonstrate that H17 is unique among characterized HAs and that the bat-derived influenza virus may use a different entry mechanism compared to canonical influenza viruses.