1. Carbohydrate-binding molecules inhibit viral fusion and entry by crosslinking membrane glycoproteins
- Author
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Myoung-Soon Cho, Yongming Xie, Kamran Melikov, Alan J. Waring, Robert I. Lehrer, Hélène Delanoë-Ayari, Joseph A. Loo, Leonid V. Chernomordik, Andrew Y. Chen, Eugenia Leikina, and Wei Wang
- Subjects
Sindbis virus ,Erythrocytes ,Immunology ,Hemagglutinins, Viral ,Hemagglutinin (influenza) ,Virus Replication ,Membrane Fusion ,Virus ,Defensins ,Anti-Infective Agents ,Orthomyxoviridae Infections ,Viral Envelope Proteins ,Cell Line, Tumor ,Humans ,Immunology and Allergy ,Membrane Glycoproteins ,Innate immune system ,biology ,Lectin ,Lipid bilayer fusion ,Orthomyxoviridae ,biology.organism_classification ,Molecular biology ,Immunity, Innate ,Cell biology ,Membrane glycoproteins ,Cell culture ,biology.protein ,Carbohydrate Metabolism ,Viral Fusion Proteins - Abstract
Defensins are peptides that protect the host against microorganisms. Here we show that the theta-defensin retrocyclin 2 (RC2) inhibited influenza virus infection by blocking membrane fusion mediated by the viral hemagglutinin. RC2 was effective even after hemagglutinin attained a fusogenic conformation or had induced membrane hemifusion. RC2, a multivalent lectin, prevented hemagglutinin-mediated fusion by erecting a network of crosslinked and immobilized surface glycoproteins. RC2 also inhibited fusion mediated by Sindbis virus and baculovirus. Human beta-defensin 3 and mannan-binding lectin also blocked viral fusion by creating a protective barricade of immobilized surface proteins. This general mechanism might explain the broad-spectrum antiviral activity of many multivalent lectins of the innate immune system.
- Published
- 2005
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