Relevance of Host Cell Surface Glycan Structure for Cell Specificity of Influenza A Viruses

Markus Kastner, Andreas Karner, Rong Zhu, Qiang Huang, Andreas Geissner, Anne Sadewasser, Markus Lesch, Xenia Wörmann, Alexander Karlas, Peter H. Seeberger, Thorsten Wolff, Peter Hinterdorfer, Andreas Herrmann, Christian Sieben

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


Influenza A viruses (IAVs) initiate infection via binding of the viral hemagglutinin (HA) to sialylated glycans on host cells. HA’s receptor specificity towards individual glycans is well studied and clearly critical for virus infection, but the contribution of the highly heterogeneous and complex glycocalyx to virus–cell adhesion remains elusive. Here, we use two complementary methods, glycan arrays and single-virus force spectroscopy (SVFS), to compare influenza virus receptor specificity with virus binding to live cells. Unexpectedly, we found that HA’s receptor binding preference does not necessarily reflect virus–cell specificity. We propose SVFS as a tool to elucidate the cell binding preference of IAVs, thereby including the complex environment of sialylated receptors within the plasma membrane of living cells.

Original languageEnglish
Article number1507
Issue number7
Publication statusPublished - Jul 2023


  • cell binding
  • force spectroscopy
  • influenza A virus
  • Hemagglutinin Glycoproteins, Influenza Virus/chemistry
  • Humans
  • Influenza, Human
  • Virus Attachment
  • Receptors, Virus/metabolism
  • Influenza A virus/metabolism
  • Polysaccharides/chemistry


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