Receptor binding by H10 influenza viruses

Sebastien G. Vachieri, Xiaoli Xiong, Patrick J. Collins, Philip A. Walker, Stephen R. Martin, Lesley F. Haire, Ying Zhang, John W. McCauley, Steven J. Gamblin () and John J. Skehel ()
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Sebastien G. Vachieri: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Xiaoli Xiong: 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
Philip A. Walker: 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
Lesley F. Haire: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Ying Zhang: 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
Steven J. Gamblin: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
John J. Skehel: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK

Nature, 2014, vol. 511, issue 7510, 475-477

Abstract: The structure and receptor-binding characteristics are presented of the haemagglutinin (HA) from an avian H10N2 virus that closely resembles an isolate from recent human fatalities; although avian H10 has a marked preference for the avian receptor, it is already able to bind to the human receptor, and its structure in complex with the human receptor shows similarities to HA from pandemic H1 and H7 viruses.

Date: 2014
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DOI: 10.1038/nature13443

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