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Functional balance between haemagglutinin and neuraminidase in influenza virus infections

Identifieur interne : 001775 ( Main/Exploration ); précédent : 001774; suivant : 001776

Functional balance between haemagglutinin and neuraminidase in influenza virus infections

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

Source :

RBID : ISTEX:CA5DF7215C4873D815400E284DEA05BBFFDA15DB

English descriptors

Abstract

Influenza A and B viruses carry two surface glycoproteins, the haemagglutinin (HA) and the neuraminidase (NA). Both proteins have been found to recognise the same host cell molecule, sialic acid. HA binds to sialic acid‐containing receptors on target cells to initiate virus infection, whereas NA cleaves sialic acids from cellular receptors and extracellular inhibitors to facilitate progeny virus release and to promote the spread of the infection to neighbouring cells. Numerous studies performed recently have revealed that an optimal interplay between these receptor‐binding and receptor‐destroying activities of the surface glycoproteins is required for efficient virus replication. An existing balance between the antagonistic HA and NA functions of individual viruses can be disturbed by various events, such as reassortment, virus transmission to a new host, or therapeutic inhibition of neuraminidase. The resulting decrease in the viral replicative fitness is usually overcome by restoration of the functional balance due to compensatory mutations in HA, NA or both proteins. Copyright © 2002 John Wiley & Sons, Ltd.

Url:
DOI: 10.1002/rmv.352


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<term>Cellular receptors</term>
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<term>Embryonated chicken eggs</term>
<term>Functional balance</term>
<term>Glycoprotein</term>
<term>Haemagglutinin</term>
<term>Hemagglutinin</term>
<term>Host cells</term>
<term>Human viruses</term>
<term>Inhibitor</term>
<term>John wiley sons</term>
<term>Mdck cells</term>
<term>Membrane fusion</term>
<term>Molecular species</term>
<term>Mutant</term>
<term>Mutation</term>
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<term>Neuraminidase activity</term>
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<term>Progeny</term>
<term>Progeny virions</term>
<term>Reassortants</term>
<term>Receptor</term>
<term>Receptor binding</term>
<term>Receptor binding site</term>
<term>Recombinant viruses</term>
<term>Replication</term>
<term>Sialic</term>
<term>Sialic acid</term>
<term>Sialic acid receptors</term>
<term>Sialic acids</term>
<term>Surface glycoproteins</term>
<term>Viral</term>
<term>Virol</term>
<term>Virology</term>
<term>Virus</term>
<term>Virus neuraminidase</term>
<term>Virus reassortants</term>
<term>Virus release</term>
<term>Virus replication</term>
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<div type="abstract" xml:lang="en">Influenza A and B viruses carry two surface glycoproteins, the haemagglutinin (HA) and the neuraminidase (NA). Both proteins have been found to recognise the same host cell molecule, sialic acid. HA binds to sialic acid‐containing receptors on target cells to initiate virus infection, whereas NA cleaves sialic acids from cellular receptors and extracellular inhibitors to facilitate progeny virus release and to promote the spread of the infection to neighbouring cells. Numerous studies performed recently have revealed that an optimal interplay between these receptor‐binding and receptor‐destroying activities of the surface glycoproteins is required for efficient virus replication. An existing balance between the antagonistic HA and NA functions of individual viruses can be disturbed by various events, such as reassortment, virus transmission to a new host, or therapeutic inhibition of neuraminidase. The resulting decrease in the viral replicative fitness is usually overcome by restoration of the functional balance due to compensatory mutations in HA, NA or both proteins. Copyright © 2002 John Wiley & Sons, Ltd.</div>
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