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Natural and synthetic sialic acid‐containing inhibitors of influenza virus receptor binding

Identifieur interne : 000747 ( Istex/Curation ); précédent : 000746; suivant : 000748

Natural and synthetic sialic acid‐containing inhibitors of influenza virus receptor binding

Auteurs : Mikhail Matrosovich [Allemagne, Russie] ; Hans-Dieter Klenk [Allemagne]

Source :

RBID : ISTEX:329DFD71D1AF6ECC4675664E080743611733EB33

English descriptors

Abstract

Influenza viruses attach to susceptible cells via multivalent interactions of their haemagglutinins with sialyloligosaccharide moieties of cellular glycoconjugates. Soluble macromolecules containing sialic acid from animal sera and mucosal fluids can act as decoy receptors and competitively inhibit virus‐mediated haemagglutination and infection. Although a role for these natural inhibitors in the innate anti‐influenza immunity is still not clear, studies are in progress on the design of synthetic sialic acid‐containing inhibitors of receptor binding which could be used as anti‐influenza drugs. Copyright © 2003 John Wiley & Sons, Ltd.

Url:
DOI: 10.1002/rmv.372

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ISTEX:329DFD71D1AF6ECC4675664E080743611733EB33

Le document en format XML

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<term>Amino</term>
<term>Analogue</term>
<term>Avian</term>
<term>Avian viruses</term>
<term>Biol</term>
<term>Bivalent</term>
<term>Bivalent sialosides</term>
<term>Bovin</term>
<term>Cell culture</term>
<term>Cellular receptors</term>
<term>Chem</term>
<term>Copyright</term>
<term>Determinant</term>
<term>Different virus strains</term>
<term>Embryonated eggs</term>
<term>Equine</term>
<term>Erythrocyte</term>
<term>Febs lett</term>
<term>Gambaryan</term>
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<term>Haemagglutination</term>
<term>Haemagglutination inhibition</term>
<term>Hemagglutinin</term>
<term>Horse serum</term>
<term>Human virus</term>
<term>Human viruses</term>
<term>Influenza virus receptor binding</term>
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<term>Monovalent sialosides</term>
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<term>Mutation</term>
<term>Natural inhibitors</term>
<term>Neu5ac</term>
<term>Neuraminidase</term>
<term>Neutralisation</term>
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<term>Penultimate sugar</term>
<term>Polyvalent</term>
<term>Receptor</term>
<term>Receptor binding</term>
<term>Replication</term>
<term>Serum inhibitors</term>
<term>Sialic</term>
<term>Sialic acid</term>
<term>Sialic acid species</term>
<term>Sialic acids</term>
<term>Sialic inhibitors</term>
<term>Sialoside</term>
<term>Sialosides</term>
<term>Sialyloligosaccharide moieties</term>
<term>Surfactant</term>
<term>Surfactant protein</term>
<term>Synthetic inhibitors</term>
<term>Synthetic sialic inhibitors</term>
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<term>Tuzikov</term>
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<term>Virol</term>
<term>Virology</term>
<term>Virus</term>
<term>Virus attachment</term>
<term>Virus binding</term>
<term>Virus hemagglutinin</term>
<term>Virus infection</term>
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<div type="abstract" xml:lang="en">Influenza viruses attach to susceptible cells via multivalent interactions of their haemagglutinins with sialyloligosaccharide moieties of cellular glycoconjugates. Soluble macromolecules containing sialic acid from animal sera and mucosal fluids can act as decoy receptors and competitively inhibit virus‐mediated haemagglutination and infection. Although a role for these natural inhibitors in the innate anti‐influenza immunity is still not clear, studies are in progress on the design of synthetic sialic acid‐containing inhibitors of receptor binding which could be used as anti‐influenza drugs. Copyright © 2003 John Wiley & Sons, Ltd.</div>
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