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

Kastner, M., Karner, A., Zhu, R., Huang, Q., Zhang, D., Liu, J., et al. (2017). Relevance of host cell surface glycan structure for cell specificity of influenza A virus. bioRxiv. doi:10.1101/203349.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-AAA6-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-60C4-0
Genre: Journal Article

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Kastner, Markus, Author
Karner, Andreas, Author
Zhu, Rong, Author
Huang, Qiang, Author
Zhang, Dandan, Author
Liu, Jianping, Author
Geissner, Andreas1, Author              
Sadewasser, Anne, Author
Lesch, Markus, Author
Woermann, Xenia, Author
Karlas, Alexander, Author
Seeberger, Peter H.2, Author              
Wolff, Thorsten, Author
Hinterdorfer, Peter, Author
Herrmann, Andreas, Author
Sieben, Christian, Author
Affiliations:
1Chakkumal Anish, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863299              
2Peter H. Seeberger - Vaccine Development, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863308              

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 Abstract: 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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 Dates: 2017
 Publication Status: Published in print
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Title: bioRxiv
Source Genre: Journal
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Publ. Info: Cold Spring Harbor : Coldl Spring Harbor Laboratory
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ZDB: 2766415-6