PoplarV1, Main, Exploration, bibRecord, 001C43

Molecular Characterisation of the Haemagglutinin Glycan-Binding Specificity of Egg-Adapted Vaccine Strains of the Pandemic 2009 H1N1 Swine Influenza A Virus.

Identifieur interne : 001C43 ( Main/Exploration ); précédent : 001C42; suivant : 001C44

Molecular Characterisation of the Haemagglutinin Glycan-Binding Specificity of Egg-Adapted Vaccine Strains of the Pandemic 2009 H1N1 Swine Influenza A Virus.

Auteurs : Vincenzo Carbone [Nouvelle-Zélande] ; Elena K. Schneider [Australie] ; Steve Rockman [Australie] ; Mark Baker [Australie] ; Johnny X. Huang [Australie] ; Chi Ong [Australie] ; Matthew A. Cooper [Australie] ; Elizabeth Yuriev [Australie] ; Jian Li [Australie] ; Tony Velkov [Australie]

Source :

Molecules (Basel, Switzerland) [ 1420-3049 ] ; 2015.

RBID : pubmed:26056814

Descripteurs français

KwdFr :
- Animaux (MeSH), Conformation des protéines (MeSH), Humains (MeSH), Hémagglutinines (composition chimique), Hémagglutinines (génétique), Hémagglutinines (métabolisme), Liaison aux protéines (MeSH), Modèles moléculaires (MeSH), Mutation (MeSH), Polyosides (composition chimique), Polyosides (métabolisme), Simulation de docking moléculaire (MeSH), Sous-type H1N1 du virus de la grippe A (physiologie), Suidae (MeSH).
MESH :
- composition chimique : Hémagglutinines, Polyosides.
- génétique : Hémagglutinines.
- métabolisme : Hémagglutinines, Polyosides.
- physiologie : Sous-type H1N1 du virus de la grippe A.
- Animaux, Conformation des protéines, Humains, Liaison aux protéines, Modèles moléculaires, Mutation, Simulation de docking moléculaire, Suidae.

English descriptors

KwdEn :
- Animals (MeSH), Hemagglutinins (chemistry), Hemagglutinins (genetics), Hemagglutinins (metabolism), Humans (MeSH), Influenza A Virus, H1N1 Subtype (physiology), Models, Molecular (MeSH), Molecular Docking Simulation (MeSH), Mutation (MeSH), Polysaccharides (chemistry), Polysaccharides (metabolism), Protein Binding (MeSH), Protein Conformation (MeSH), Swine (MeSH).
MESH :
- chemical , chemistry : Hemagglutinins, Polysaccharides.
- chemical , genetics : Hemagglutinins.
- chemical , metabolism : Hemagglutinins, Polysaccharides.
- physiology : Influenza A Virus, H1N1 Subtype.
- Animals, Humans, Models, Molecular, Molecular Docking Simulation, Mutation, Protein Binding, Protein Conformation, Swine.

Abstract

The haemagglutinin (HA) glycan binding selectivity of H1N1 influenza viruses is an important determinant for the host range of the virus and egg-adaption during vaccine production. This study integrates glycan binding data with structure-recognition models to examine the impact of the K123N, D225G and Q226R mutations (as seen in the HA of vaccine strains of the pandemic 2009 H1N1 swine influenza A virus). The glycan-binding selectivity of three A/California/07/09 vaccine production strains, and purified recombinant A/California/07/09 HAs harboring these mutations was examined via a solid-phase ELISA assay. Wild-type A/California/07/09 recombinant HA bound specifically to α2,6-linked sialyl-glycans, with no affinity for the α2,3-linked sialyl-glycans in the array. In contrast, the vaccine virus strains and recombinant HA harboring the Q226R HA mutation displayed a comparable pattern of highly specific binding to α2,3-linked sialyl-glycans, with a negligible affinity for α2,6-linked sialyl-glycans. The D225G A/California/07/09 recombinant HA displayed an enhanced binding affinity for both α2,6- and α2,3-linked sialyl-glycans in the array. Notably its α2,6-glycan affinity was generally higher compared to its α2,3-glycan affinity, which may explain why the double mutant was not naturally selected during egg-adaption of the virus. The K123N mutation which introduces a glycosylation site proximal to the receptor binding site, did not impact the α2,3/α2,6 glycan selectivity, however, it lowered the overall glycan binding affinity of the HA; suggesting glycosylation may interfere with receptor binding. Docking models and 'per residues' scoring were employed to provide a structure-recognition rational for the experimental glycan binding data. Collectively, the glycan binding data inform future vaccine design strategies to introduce the D225G or Q226R amino acid substitutions into recombinant H1N1 viruses.

DOI: 10.3390/molecules200610415
PubMed: 26056814
PubMed Central: PMC6272818

Affiliations:

Australie, Nouvelle-Zélande

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

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Le document en format XML

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<term>Hemagglutinins (genetics)</term>
<term>Hemagglutinins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Influenza A Virus, H1N1 Subtype (physiology)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Docking Simulation (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Polysaccharides (chemistry)</term>
<term>Polysaccharides (metabolism)</term>
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<term>Conformation des protéines (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Hémagglutinines (composition chimique)</term>
<term>Hémagglutinines (génétique)</term>
<term>Hémagglutinines (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
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<term>Mutation (MeSH)</term>
<term>Polyosides (composition chimique)</term>
<term>Polyosides (métabolisme)</term>
<term>Simulation de docking moléculaire (MeSH)</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Hémagglutinines</term>
<term>Polyosides</term>
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<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
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<front><div type="abstract" xml:lang="en">The haemagglutinin (HA) glycan binding selectivity of H1N1 influenza viruses is an important determinant for the host range of the virus and egg-adaption during vaccine production. This study integrates glycan binding data with structure-recognition models to examine the impact of the K123N, D225G and Q226R mutations (as seen in the HA of vaccine strains of the pandemic 2009 H1N1 swine influenza A virus). The glycan-binding selectivity of three A/California/07/09 vaccine production strains, and purified recombinant A/California/07/09 HAs harboring these mutations was examined via a solid-phase ELISA assay. Wild-type A/California/07/09 recombinant HA bound specifically to α2,6-linked sialyl-glycans, with no affinity for the α2,3-linked sialyl-glycans in the array. In contrast, the vaccine virus strains and recombinant HA harboring the Q226R HA mutation displayed a comparable pattern of highly specific binding to α2,3-linked sialyl-glycans, with a negligible affinity for α2,6-linked sialyl-glycans. The D225G A/California/07/09 recombinant HA displayed an enhanced binding affinity for both α2,6- and α2,3-linked sialyl-glycans in the array. Notably its α2,6-glycan affinity was generally higher compared to its α2,3-glycan affinity, which may explain why the double mutant was not naturally selected during egg-adaption of the virus. The K123N mutation which introduces a glycosylation site proximal to the receptor binding site, did not impact the α2,3/α2,6 glycan selectivity, however, it lowered the overall glycan binding affinity of the HA; suggesting glycosylation may interfere with receptor binding. Docking models and 'per residues' scoring were employed to provide a structure-recognition rational for the experimental glycan binding data. Collectively, the glycan binding data inform future vaccine design strategies to introduce the D225G or Q226R amino acid substitutions into recombinant H1N1 viruses. </div>
</front>
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<Abstract><AbstractText>The haemagglutinin (HA) glycan binding selectivity of H1N1 influenza viruses is an important determinant for the host range of the virus and egg-adaption during vaccine production. This study integrates glycan binding data with structure-recognition models to examine the impact of the K123N, D225G and Q226R mutations (as seen in the HA of vaccine strains of the pandemic 2009 H1N1 swine influenza A virus). The glycan-binding selectivity of three A/California/07/09 vaccine production strains, and purified recombinant A/California/07/09 HAs harboring these mutations was examined via a solid-phase ELISA assay. Wild-type A/California/07/09 recombinant HA bound specifically to α2,6-linked sialyl-glycans, with no affinity for the α2,3-linked sialyl-glycans in the array. In contrast, the vaccine virus strains and recombinant HA harboring the Q226R HA mutation displayed a comparable pattern of highly specific binding to α2,3-linked sialyl-glycans, with a negligible affinity for α2,6-linked sialyl-glycans. The D225G A/California/07/09 recombinant HA displayed an enhanced binding affinity for both α2,6- and α2,3-linked sialyl-glycans in the array. Notably its α2,6-glycan affinity was generally higher compared to its α2,3-glycan affinity, which may explain why the double mutant was not naturally selected during egg-adaption of the virus. The K123N mutation which introduces a glycosylation site proximal to the receptor binding site, did not impact the α2,3/α2,6 glycan selectivity, however, it lowered the overall glycan binding affinity of the HA; suggesting glycosylation may interfere with receptor binding. Docking models and 'per residues' scoring were employed to provide a structure-recognition rational for the experimental glycan binding data. Collectively, the glycan binding data inform future vaccine design strategies to introduce the D225G or Q226R amino acid substitutions into recombinant H1N1 viruses. </AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Carbone</LastName>
<ForeName>Vincenzo</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>AgResearch Limited, Grasslands Research Centre, Tennent Drive, Private Bag 11008, Palmerston North 4442, New Zealand. Vince.Carbone@agresearch.co.nz.</Affiliation>
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   |texte=   Molecular Characterisation of the Haemagglutinin Glycan-Binding Specificity of Egg-Adapted Vaccine Strains of the Pandemic 2009 H1N1 Swine Influenza A Virus.
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Molecular Characterisation of the Haemagglutinin Glycan-Binding Specificity of Egg-Adapted Vaccine Strains of the Pandemic 2009 H1N1 Swine Influenza A Virus.

Molecular Characterisation of the Haemagglutinin Glycan-Binding Specificity of Egg-Adapted Vaccine Strains of the Pandemic 2009 H1N1 Swine Influenza A Virus.

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