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

Abstract

first_page settings Order Article Reprints Open AccessHypothesis Relevance of Host Cell Surface Glycan Structure for Cell Specificity of Influenza A Viruses by Markus Kastner 1,†,‡, Andreas Karner 1,†,§ [ORCID] , Rong Zhu 1,† [ORCID] , Qiang Huang 2 [ORCID] , Andreas Geissner 3,4,‖, Anne Sadewasser 5,¶, Markus Lesch 6, Xenia Wörmann 6, Alexander Karlas 6,**, Peter H. Seeberger 3,4 [ORCID] , Thorsten Wolff 5 [ORCID] , Peter Hinterdorfer 1 [ORCID] , Andreas Herrmann 7 and Christian Sieben 8,9,* [ORCID] 1 Institute for Biophysics, Johannes Kepler University Linz, 4020 Linz, Austria 2 State Key Laboratory of Genetic Engineering, Shanghai Engineering Research Center of Industrial Microorganisms, MOE Engineering Research Center of Gene Technology, School of Life Sciences, Fudan University, Shanghai 200438, China 3 Department for Biomolecular Systems, Max Planck Institute for Colloids and Interfaces, 14476 Potsdam, Germany 4 Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany 5 Division of Influenza and other Respiratory Viruses, Robert Koch-Institute, 13353 Berlin, Germany 6 Molecular Biology Department, Max Planck Institute for Infection Biology, 10117 Berlin, Germany 7 Institut für Chemie und Biochemie, Freie Universität Berlin, Altensteinstraße 23a, 14195 Berlin, Germany 8 Nanoscale Infection Biology Group, Department of Cell Biology, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany 9 Institute for Genetics, Technische Universität Braunschweig, 38106 Braunschweig, Germany * Author to whom correspondence should be addressed. † These authors contributed equally to this work. ‡ Current address: Materials Characterization Lab (MCL), Materials Research Institute (MRI), Pennsylvania State University, University Park, PA 16802, USA. § Current address: University of Applied Sciences Upper Austria, School of Medical Engineering and Applied Social Sciences, Garnisonstr. 21, 4020 Linz, Austria. ‖ Current address: Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC V6T 1Z1, Canada. ¶ Current address: Secarna Pharmaceuticals GmbH & Co. KG, Am Klopferspitz 19, 82152 Planegg, Germany. ** Current address: Viral Vectors and Gene Therapeutics, ProBioGen AG, 13086 Berlin, Germany. Viruses 2023, 15(7), 1507; https://doi.org/10.3390/v15071507 Received: 9 May 2023 / Revised: 21 June 2023 / Accepted: 28 June 2023 / Published: 5 July 2023 (This article belongs to the Special Issue Physical Virology - Viruses at Multiple Levels of Complexity) Download Browse Figures Review Reports Versions Notes Abstract 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