Comparison of the receptor binding properties of contemporary swine isolates and early human pandemic H1N1 isolates (Novel 2009 H1N1)

Konrad C. Bradley, Cheryl A. Jones, S. Mark Tompkins, Ralph A. Tripp, Rupert J. Russell, Marie R. Gramer, Jamie Heimburg-Molinaro, David F. Smith, Richard D. Cummings, David A. Steinhauer

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Abstract

We have utilized glycan microarray technology to determine the receptor binding properties of early isolates from the recent 2009 H1N1 human pandemic (pdmH1N1), and compared them to North American swine influenza isolates from the same year, as well as past seasonal H1N1 human isolates. We showed that the pdmH1N1 strains, as well as the swine influenza isolates examined, bound almost exclusively to glycans with α2,6-linked sialic acid with little binding detected for α2,3-linked species. This is highlighted by pair-wise comparisons between compounds with identical glycan backbones, differing only in the chemistry of their terminal linkages. The overall similarities in receptor binding profiles displayed by pdmH1N1 strains and swine isolates indicate that little or no adaptation appeared to be necessary in the binding component of HA for transmission from pig to human, and subsequent human to human spread.

Original languageEnglish (US)
Pages (from-to)169-182
Number of pages14
JournalVirology
Volume413
Issue number2
DOIs
StatePublished - May 10 2011

Bibliographical note

Funding Information:
Support for our work has been provided by NIH/NIAID contract HHSN2662007000006C . We would also like to thank members of the Steinhauer, Tompkins, and Tripp laboratory for useful comments on this manuscript. The authors would also like to acknowledge The Consortium for Functional Glycomics funded by the NIGMS GM62116 for support of the glycan array analysis.

Keywords

  • Glycan microarray
  • Hemagglutinin
  • Influenza
  • Receptor binding
  • Swine influenza

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