Serveur d'exploration H2N2

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Adaptation of novel H7N9 influenza A virus to human receptors

Identifieur interne : 000919 ( Main/Exploration ); précédent : 000918; suivant : 000920

Adaptation of novel H7N9 influenza A virus to human receptors

Auteurs : J. C. F. M. Dortmans [Pays-Bas] ; J. Dekkers [Pays-Bas] ; I. N. Ambepitiya Wickramasinghe [Pays-Bas] ; M. H. Verheije [Pays-Bas] ; P. J. M. Rottier [Pays-Bas] ; F. J. M. Van Kuppeveld [Pays-Bas] ; E. De Vries [Pays-Bas] ; C. A. M. De Haan [Pays-Bas]

Source :

RBID : PMC:3808826

Abstract

The emergence of the novel H7N9 influenza A virus (IAV) has caused global concerns about the ability of this virus to spread between humans. Analysis of the receptor-binding properties of this virus using a recombinant protein approach in combination with fetuin-binding, glycan array and human tissue-binding assays demonstrates increased binding of H7 to both α2-6 and α2-8 sialosides as well as reduced binding to α2-3-linked SIAs compared to a closely related avian H7N9 virus from 2008. These differences could be attributed to substitutions Q226L and G186V. Analysis of the enzymatic activity of the neuraminidase N9 protein indicated a reduced sialidase activity, consistent with the reduced binding of H7 to α2-3 sialosides. However, the novel H7N9 virus still preferred binding to α2-3- over α2-6-linked SIAs and was not able to efficiently bind to epithelial cells of human trachea in contrast to seasonal IAV, consistent with its limited human-to-human transmission.


Url:
DOI: 10.1038/srep03058
PubMed: 24162312
PubMed Central: 3808826


Affiliations:


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


Le document en format XML

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<p>The emergence of the novel H7N9 influenza A virus (IAV) has caused global concerns about the ability of this virus to spread between humans. Analysis of the receptor-binding properties of this virus using a recombinant protein approach in combination with fetuin-binding, glycan array and human tissue-binding assays demonstrates increased binding of H7 to both α2-6 and α2-8 sialosides as well as reduced binding to α2-3-linked SIAs compared to a closely related avian H7N9 virus from 2008. These differences could be attributed to substitutions Q226L and G186V. Analysis of the enzymatic activity of the neuraminidase N9 protein indicated a reduced sialidase activity, consistent with the reduced binding of H7 to α2-3 sialosides. However, the novel H7N9 virus still preferred binding to α2-3- over α2-6-linked SIAs and was not able to efficiently bind to epithelial cells of human trachea in contrast to seasonal IAV, consistent with its limited human-to-human transmission.</p>
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<name sortKey="Zhang, T" uniqKey="Zhang T">T. Zhang</name>
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<name sortKey="Dortmans, J C F M" sort="Dortmans, J C F M" uniqKey="Dortmans J" first="J. C. F. M." last="Dortmans">J. C. F. M. Dortmans</name>
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<name sortKey="De Vries, E" sort="De Vries, E" uniqKey="De Vries E" first="E." last="De Vries">E. De Vries</name>
<name sortKey="Dekkers, J" sort="Dekkers, J" uniqKey="Dekkers J" first="J." last="Dekkers">J. Dekkers</name>
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