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Abstract

H10N8 follows H7N9 and H5N1 as the latest in a line of avian influenza viruses that cause serious disease in humans and have become a threat to public health1. Since December 2013, three human cases of H10N8 infection have been reported, two of whom are known to have died. To gather evidence relating to the epidemic potential of H10 we have determined the structure of the haemagglutinin of a previously isolated avian H10 virus and we present here results relating especially to its receptor-binding properties, as these are likely to be major determinants of virus transmissibility. Our results show, first, that the H10 virus possesses high avidity for human receptors and second, from the crystal structure of the complex formed by avian H10 haemagglutinin with human receptor, it is clear that the conformation of the bound receptor has characteristics of both the 1918 H1N1 pandemic virus2 and the human H7 viruses isolated from patients in 2013 (ref. 3). We conclude that avian H10N8 virus has sufficient avidity for human receptors to account for its infection of humans but that its preference for avian receptors should make avian-receptor-rich human airway mucins4 an effective block to widespread infection. In terms of surveillance, particular attention will be paid to the detection of mutations in the receptor-binding site of the H10 haemagglutinin that decrease its avidity for avian receptor, and could enable it to be more readily transmitted between humans.

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Change history

  • 23 July 2014

    An error was corrected in the legend for Extended Data Fig. 4.

Accessions

Data deposits

Structural data have been deposited with the Protein Data Bank under accession numbers 4CYV, 4CYW, 4CYZ, 4CZ0 and 4D00.

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Acknowledgements

We thank N. Bovin for gifts of sulphated sialoside. We greatly acknowledge Diamond Light Source for access to synchrotron time under proposal 7707. This work was funded by the Medical Research Council through programmes U117584222, U117570592 and U117585868.

Author information

Author notes

    • Sebastien G. Vachieri
    •  & Xiaoli Xiong

    These authors contributed equally to this work.

Affiliations

  1. MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK

    • 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
    •  & John J. Skehel

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Contributions

All authors performed experiments and contributed to the writing of the manuscript.

Competing interests

The authors declare no competing financial interests.

Corresponding authors

Correspondence to Steven J. Gamblin or John J. Skehel.

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https://doi.org/10.1038/nature13443

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