StressCovidV1, Ncbi, Merge, bibRecord, 000463

Structural basis and sequence co-evolution analysis of the hemagglutinin protein of pandemic influenza A/H1N1 (2009) virus.

Identifieur interne : 000463 ( Ncbi/Merge ); précédent : 000462; suivant : 000464

Structural basis and sequence co-evolution analysis of the hemagglutinin protein of pandemic influenza A/H1N1 (2009) virus.

Auteurs : Herman Tse ; Richard Y T. Kao ; Wai Lan Wu ; Wilian W L. Lim ; Honglin Chen ; Ming Yiu Yeung ; Patrick C Y. Woo ; Kong-Hung Sze ; Kwok-Yung Yuen

Source :

Experimental biology and medicine (Maywood, N.J.) [ 1535-3699 ] ; 2011.

RBID : pubmed:21727184

Descripteurs français

English descriptors

KwdEn :
- Binding Sites, Disease Outbreaks, Evolution, Molecular, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Humans, Influenza A Virus, H1N1 Subtype (genetics), Influenza A Virus, H1N1 Subtype (immunology), Models, Molecular, Pandemics, Protein Conformation, Sequence Analysis.
MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , genetics : Hemagglutinin Glycoproteins, Influenza Virus.
- genetics : Influenza A Virus, H1N1 Subtype.
- immunology : Influenza A Virus, H1N1 Subtype.
- Binding Sites, Disease Outbreaks, Evolution, Molecular, Humans, Models, Molecular, Pandemics, Protein Conformation, Sequence Analysis.

Abstract

Severe pandemic influenza A H1N1 (2009) infection, especially in the lower respiratory tract, is often associated with the virus carrying a D222G substitution in the hemagglutinin (HA) protein of the virus. The mechanism for this association has not been fully explored. In the in vitro binding assay, it was found that clinical isolates carrying D222G substitution exhibit higher binding avidity to 2,3-linked sialic acids than the wild-type virus. The receptor binding pocket of the pandemic influenza (H1N1) HA was found to be smaller than those of other influenza A strains, allowing tighter binding of the virus with the receptor, yet also inducing steric stress for the binding. Our homology modeling and molecular docking calculations implicated that residue 222 may affect the positioning of the conserved Q223 residue, hence modulating flexibility of the binding pocket and steric hindrance during receptor binding. The molecular property of residue 222 can also directly influence the 'lysine fence' via the polarity of the amino acid residue where D222G substitution will enhance the electrostatic interactions between the receptor and the protein. The potential importance of residue 222 was illustrated by evolutionary analysis, which showed that this site is under intense selection pressure during adaptation of the virus to human host. Our findings provide a useful reference for follow-up studies in monitoring the ongoing evolution of the pandemic influenza A H1N1 (2009) virus.

DOI: 10.1258/ebm.2011.010264
PubMed: 21727184

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Le document en format XML

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<term>Hemagglutinin Glycoproteins, Influenza Virus (genetics)</term>
<term>Humans</term>
<term>Influenza A Virus, H1N1 Subtype (genetics)</term>
<term>Influenza A Virus, H1N1 Subtype (immunology)</term>
<term>Models, Molecular</term>
<term>Pandemics</term>
<term>Protein Conformation</term>
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<term>Conformation des protéines</term>
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<term>Glycoprotéine hémagglutinine du virus influenza (génétique)</term>
<term>Humains</term>
<term>Modèles moléculaires</term>
<term>Pandémies</term>
<term>Sites de fixation</term>
<term>Sous-type H1N1 du virus de la grippe A (génétique)</term>
<term>Sous-type H1N1 du virus de la grippe A (immunologie)</term>
<term>Évolution moléculaire</term>
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<term>Models, Molecular</term>
<term>Pandemics</term>
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<term>Sequence Analysis</term>
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<term>Conformation des protéines</term>
<term>Flambées de maladies</term>
<term>Glycoprotéine hémagglutinine du virus influenza</term>
<term>Humains</term>
<term>Modèles moléculaires</term>
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<front><div type="abstract" xml:lang="en">Severe pandemic influenza A H1N1 (2009) infection, especially in the lower respiratory tract, is often associated with the virus carrying a D222G substitution in the hemagglutinin (HA) protein of the virus. The mechanism for this association has not been fully explored. In the in vitro binding assay, it was found that clinical isolates carrying D222G substitution exhibit higher binding avidity to 2,3-linked sialic acids than the wild-type virus. The receptor binding pocket of the pandemic influenza (H1N1) HA was found to be smaller than those of other influenza A strains, allowing tighter binding of the virus with the receptor, yet also inducing steric stress for the binding. Our homology modeling and molecular docking calculations implicated that residue 222 may affect the positioning of the conserved Q223 residue, hence modulating flexibility of the binding pocket and steric hindrance during receptor binding. The molecular property of residue 222 can also directly influence the 'lysine fence' via the polarity of the amino acid residue where D222G substitution will enhance the electrostatic interactions between the receptor and the protein. The potential importance of residue 222 was illustrated by evolutionary analysis, which showed that this site is under intense selection pressure during adaptation of the virus to human host. Our findings provide a useful reference for follow-up studies in monitoring the ongoing evolution of the pandemic influenza A H1N1 (2009) virus.</div>
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<Abstract><AbstractText>Severe pandemic influenza A H1N1 (2009) infection, especially in the lower respiratory tract, is often associated with the virus carrying a D222G substitution in the hemagglutinin (HA) protein of the virus. The mechanism for this association has not been fully explored. In the in vitro binding assay, it was found that clinical isolates carrying D222G substitution exhibit higher binding avidity to 2,3-linked sialic acids than the wild-type virus. The receptor binding pocket of the pandemic influenza (H1N1) HA was found to be smaller than those of other influenza A strains, allowing tighter binding of the virus with the receptor, yet also inducing steric stress for the binding. Our homology modeling and molecular docking calculations implicated that residue 222 may affect the positioning of the conserved Q223 residue, hence modulating flexibility of the binding pocket and steric hindrance during receptor binding. The molecular property of residue 222 can also directly influence the 'lysine fence' via the polarity of the amino acid residue where D222G substitution will enhance the electrostatic interactions between the receptor and the protein. The potential importance of residue 222 was illustrated by evolutionary analysis, which showed that this site is under intense selection pressure during adaptation of the virus to human host. Our findings provide a useful reference for follow-up studies in monitoring the ongoing evolution of the pandemic influenza A H1N1 (2009) virus.</AbstractText>
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<name sortKey="Lim, Wilian W L" sort="Lim, Wilian W L" uniqKey="Lim W" first="Wilian W L" last="Lim">Wilian W L. Lim</name>
<name sortKey="Sze, Kong Hung" sort="Sze, Kong Hung" uniqKey="Sze K" first="Kong-Hung" last="Sze">Kong-Hung Sze</name>
<name sortKey="Tse, Herman" sort="Tse, Herman" uniqKey="Tse H" first="Herman" last="Tse">Herman Tse</name>
<name sortKey="Woo, Patrick C Y" sort="Woo, Patrick C Y" uniqKey="Woo P" first="Patrick C Y" last="Woo">Patrick C Y. Woo</name>
<name sortKey="Wu, Wai Lan" sort="Wu, Wai Lan" uniqKey="Wu W" first="Wai Lan" last="Wu">Wai Lan Wu</name>
<name sortKey="Yeung, Ming Yiu" sort="Yeung, Ming Yiu" uniqKey="Yeung M" first="Ming Yiu" last="Yeung">Ming Yiu Yeung</name>
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Structural basis and sequence co-evolution analysis of the hemagglutinin protein of pandemic influenza A/H1N1 (2009) virus.

Structural basis and sequence co-evolution analysis of the hemagglutinin protein of pandemic influenza A/H1N1 (2009) virus.

Source :

Descripteurs français

English descriptors

Abstract

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

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki