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Receptor binding by a ferret-transmissible H5 avian influenza virus

Author

Listed:
  • 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
    Present address: Laboratory of Protein Engineering and Vaccines, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.)

  • 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)

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.

Suggested Citation

  • 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 & Steven, 2013. "Receptor binding by a ferret-transmissible H5 avian influenza virus," Nature, Nature, vol. 497(7449), pages 392-396, May.
    • Handle: RePEc:nat:nature:v:497:y:2013:i:7449:d:10.1038_nature12144
    DOI: 10.1038/nature12144
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    Cited by:

    1. Simon J. L. Petitjean & Wenzhang Chen & Melanie Koehler & Ravikumar Jimmidi & Jinsung Yang & Danahe Mohammed & Blinera Juniku & Megan L. Stanifer & Steeve Boulant & Stéphane P. Vincent & David Alsteen, 2022. "Multivalent 9-O-Acetylated-sialic acid glycoclusters as potent inhibitors for SARS-CoV-2 infection," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Mengying Liu & Liane Z. X. Huang & Anthony A. Smits & Christian Büll & Yoshiki Narimatsu & Frank J. M. Kuppeveld & Henrik Clausen & Cornelis A. M. Haan & Erik Vries, 2022. "Human-type sialic acid receptors contribute to avian influenza A virus binding and entry by hetero-multivalent interactions," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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