Journal article

A Single Amino Acid Substitution in the Hemagglutinin of H3N2 Subtype Influenza A Viruses Is Associated with Resistance to the Long Pentraxin PTX3 and Enhanced Virulence in Mice

Emma R Job, Barbara Bottazzi, Kirsty R Short, Yi-Mo Deng, Alberto Mantovani, Andrew G Brooks, Patrick C Reading



The long pentraxin, pentraxin 3 (PTX3), can play beneficial or detrimental roles during infection and disease by modulating various aspects of the immune system. There is growing evidence to suggest that PTX3 can mediate antiviral activity in vitro and in vivo. Previous studies demonstrated that PTX3 and the short pentraxin serum amyloid P express sialic acids that are recognized by the hemagglutinin (HA) glycoprotein of certain influenza A viruses (IAV), resulting in virus neutralization and anti-IAV activity. In this study, we demonstrate that specificity of both HA and the viral neuraminidase for particular sialic acid linkages determines the susceptibility of H1N1, H3N2, and H7N9 strains..

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Awarded by National Health and Medical Research Council of Australia

Awarded by European Commission

Funding Acknowledgements

This work was supported by Project Grant 1032079 from the National Health and Medical Research Council of Australia. The Melbourne World Health Organization Collaborating Centre for Reference and Research on Influenza is supported by the Australian Government Department of Health. A.M. gratefully acknowledges the financial support of the European Research Council (Project HIIS) and the European Commission (FP7-HEALTH-2011-ADITEC-280873).