| 论文题目: | 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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| 作者: | Sun Xiaoman, Shi Yi, Lu Xishan, He Jianhua, Gao Feng, Yan Jinghua, Qi Jianxun, George F Gao |
| 联系作者: | George F Gao |
| 刊物名称: | Cell reports |
| 期: | 3 |
| 卷: | 3 |
| 页: | 769-78 |
| 年份: | 2013 |
| 影响因子: | - |
| 论文下载: | 下载地址 |
| 摘要: | 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 A 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 alpha2,6 SA-linkage or avian alpha2,3 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. |
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