Receptor binding by a ferret-transmissible H5 avian influenza virus

Xiaoli Xiong, Peter J. Coombs, Stephen R. Martin, Junfeng Liu, Haixia Xiao, John W. McCauley, Kathrin Locher, Philip A. Walker, Patrick J. Collins, Yoshihiro Kawaoka, John J. Skehel () and Steven J. Gamblin ()
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Xiaoli Xiong: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Peter J. Coombs: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Stephen R. Martin: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Junfeng Liu: Ministry of Agriculture, Key Laboratory of Plant Pathology, China Agricultural University, Yuanmingyuanxilu, 2, Beijing 100193, China
Haixia Xiao: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
John W. McCauley: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Kathrin Locher: Novartis Institutes for BioMedical Research, Klybeckstrasse 141, CH-4057 Basel, Switzerland
Philip A. Walker: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Patrick J. Collins: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Yoshihiro Kawaoka: University of Wisconsin-Madison
John J. Skehel: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Steven J. Gamblin: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK

Nature, 2013, vol. 497, issue 7449, 392-396

Abstract: Building on previous work that identified a mutant avian H5 virus that is transmissible between ferrets, the authors present an algorithm to predict virus avidity from the affinity of single haemagglutinin (HA)–receptor interactions; these studies predict that the mutant has a 200-fold preference for the human over the avian receptor, and crystal structures of the mutant HA in complex with human and avian receptors shed light on the molecular basis for these altered binding properties.

Date: 2013
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DOI: 10.1038/nature12144

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