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Bat-Derived Influenza Hemagglutinin H17 Does Not Bind Canonical Avian or Human Receptors and Most Likely Uses a Unique Entry Mechanism
Authors:Xiaoman Sun,Yi Shi,Xishan Lu,Jianhua He,Feng Gao,Jinghua Yan,Jianxun Qi,George   F. Gao
Affiliation:1. CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China;2. Research Network of Immunity and Health, Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China;3. University of Chinese Academy of Sciences, Beijing 100049, China;4. Laboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China;5. College of Veterinary Medicine, China Agricultural University, Beijing 100193, China;6. Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201204, China;7. National Institute For Viral Disease Control and Prevention, Chinese Center For Disease Control and Prevention, Beijing 102206, China
Abstract:
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  • Highlights? Bat influenza H17 lacks canonical human or avian receptor binding capacity ? H17 has a distorted receptor binding site with negatively charged residues ? H17 displayed trypsin susceptibility and instability even at pH 8.0 ? An exposed fusion peptide is observed in H17 structure due to contorted trimerization
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