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Relevance of host cell surface glycan structure for cell specificity of influenza A virus

By Markus Kastner, Andreas Karner, Rong Zhu, Qiang Huang, Dandan Zhang, Jianping Liu, Andreas Geissner, Anne Sadewasser, Markus Lesch, Xenia W├Ârmann, Alexander Karlas, Peter Seeberger, Thorsten Wolff, Peter Hinterdorfer, Andreas Herrmann, Christian Sieben

Posted 14 Oct 2017
bioRxiv DOI: 10.1101/203349

Influenza A viruses (IAV) initiate infection via binding of the viral hemagglutinin (HA) to sialylated glycan receptors on host cells. HAs receptor specificity towards sialic acid (SA) is well studied and clearly critical for virus infection, but the contribution of the highly complex cellular plasma membrane to the cellular specificity remains elusive. In addition, some studies indicated that other host cell factors such as the epidermal growth factor receptor might contribute to the initial virus-cell contact and further downstream signaling. Here we use two complementary methods, glycan arrays and single-virus force spectroscopy (SVFS) to compare influenza virus receptor specificity with actual host cell binding. Unexpectedly, our study reveals that HAs receptor binding preference does not necessarily reflect virus-cell specificity. We propose SVFS as a tool to elucidate the cell binding preference of IAV thereby including the complex environment of sialylated receptors within the plasma membrane of living cells.

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