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Proc Natl Acad Sci U S A. 2012 Aug 21;109(34):13626-31. doi: 10.1073/pnas.1120265109. Epub 2012 Aug 6.

Influenza virus binds its host cell using multiple dynamic interactions.

Author information

1
Department of Biology, Molecular Biophysics, Humboldt University Berlin, 10115 Berlin, Germany.

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.

PMID:
22869709
PMCID:
PMC3427095
DOI:
10.1073/pnas.1120265109
[Indexed for MEDLINE]
Free PMC Article

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