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  Influenza virus binds its host cell using multiple dynamic interactions.

Sieben, C., Kappel, C., Zhu, R., Wozniak, A., Rankl, C., Hinterdorfer, P., et al. (2012). Influenza virus binds its host cell using multiple dynamic interactions. Proceedings of the National Academy of Sciences of the United States of America, 106(34), 13626-13631. doi:10.1073/pnas.1120265109.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-ECC0-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C709-B
Genre: Journal Article

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 Creators:
Sieben, C., Author
Kappel, C.1, Author              
Zhu, R., Author
Wozniak, A., Author
Rankl, C., Author
Hinterdorfer, P., Author
Grubmüller, H.1, Author              
Herrmann, A., Author
Affiliations:
1Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              

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Free keywords: Multivalency; adhesion; avidity; tropism
 Abstract: Influenza virus belongs to a wide range of enveloped viruses. The major spike protein hemagglutinin binds sialic acid residues of glycoproteins and glycolipids with dissociation constants in the millimolar range [Sauter NK, et al. (1992) Biochemistry 31:9609–9621], indicating a multivalent binding mode. Here, we characterized the attachment of influenza virus to host cell receptors using three independent approaches. Optical tweezers and atomic force microscopy-based single-molecule force spectroscopy revealed very low interaction forces. Further, the observation of sequential unbinding events strongly suggests a multivalent binding mode between virus and cell membrane. Molecular dynamics simulations reveal a variety of unbinding pathways that indicate a highly dynamic interaction between HA and its receptor, allowing rationalization of influenza virus–cell binding quantitatively at the molecular level.

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Language(s): eng - English
 Dates: 2012-08-062012-08-21
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1120265109
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 106 (34) Sequence Number: - Start / End Page: 13626 - 13631 Identifier: -