Structure and receptor-binding properties of an airborne transmissible avian influenza A virus hemagglutinin H5 (VN1203mut)

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• 作者：Xishan Lu (13906) (33906)
  Yi Shi (23906)
  Wei Zhang (33906) (43906)
  Yanfang Zhang (53906)
  Jianxun Qi (33906)
  George F. Gao (13906) (23906) (33906) (43906) (53906) (63906)
  
• 关键词：airborne ; transmission ; H5 ; avian influenza ; structure ; receptor binding
• 刊名：Protein & Cell
• 出版年：2013
• 出版时间：July 2013
• 年：2013
• 卷：4
• 期：7
• 页码：502-511
• 全文大小：846KB
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• 作者单位：Xishan Lu (13906) (33906)
  Yi Shi (23906)
  Wei Zhang (33906) (43906)
  Yanfang Zhang (53906)
  Jianxun Qi (33906)
  George F. Gao (13906) (23906) (33906) (43906) (53906) (63906)
  
  13906. College of Veterinary Medicine, China Agricultural University, Beijing, 100193, China
  33906. CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China
  23906. Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing, 100101, China
  43906. University of Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing, 100049, China
  53906. Laboratory of Protein Engineering and Vaccines, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308, China
  63906. National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing, 102206, China
  

文摘

Avian influenza A virus continues to pose a global threat with occasional H5N1 human infections, which is emphasized by a recent severe human infection caused by avian-origin H7N9 in China. Luckily these viruses do not transmit efficiently in human populations. With a few amino acid substitutions of the hemagglutinin H5 protein in the laboratory, two H5 mutants have been shown to obtain an air-borne transmission in a mammalian ferret model. Here in this study one of the mutant H5 proteins developed by Kawaoka’s group (VN1203mut) was expressed in a baculovirus system and its receptor-binding properties were assessed. We herein show that the VN1203mut had a dramatically reduced binding affinity for the avian α2,3-linkage receptor compared to wild type but showed no detectable increase in affinity for the human α2,6-linkage receptor, using Surface Plasmon Resonance techonology. Further, the crystal structures of the VN1203mut and its complexes with either human or avian receptors demonstrate that the VN1203mut binds the human receptor in the same binding manner (cis conformation) as seen for the HAs of previously reported 1957 and 1968 pandemic influenza viruses. Our receptor binding and crystallographic data shown here further confirm that the ability to bind the avian receptor has to decrease for a higher human receptor binding affinity. As the Q226L substitution is shown important for obtaining human receptor binding, we suspect that the newly emerged H7N9 binds human receptor as H7 has a Q226L substitution.