H2N2V1, 1968, Analysis, bibRecord, 000092

Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity

Identifieur interne : 000092 ( 1968/Analysis ); précédent : 000091; suivant : 000093

Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity

Auteurs : James Stevens [États-Unis] ; Ola Blixt [États-Unis] ; Li-Mei Chen [États-Unis] ; Ruben O. Donis [États-Unis] ; James C. Paulson [États-Unis] ; Ian A. Wilson [États-Unis]

Source :

Journal of molecular biology [ 0022-2836 ] ; 2008.

RBID : PMC:2519951

Descripteurs français

KwdFr :
- Animaux, Glycoprotéine hémagglutinine du virus influenza (), Glycoprotéine hémagglutinine du virus influenza (génétique), Humains, Ligands, Maladies virales (virologie), Modèles moléculaires, Mutation (génétique), Oiseaux (virologie), Phylogénie, Polyosides (), Polyosides (métabolisme), Récepteurs viraux (métabolisme), Sous-type H5N1 du virus de la grippe A (métabolisme), Structure secondaire des protéines.
MESH :
- génétique : Glycoprotéine hémagglutinine du virus influenza, Mutation.
- métabolisme : Polyosides, Récepteurs viraux, Sous-type H5N1 du virus de la grippe A.
- virologie : Maladies virales, Oiseaux.
- Animaux, Glycoprotéine hémagglutinine du virus influenza, Humains, Ligands, Modèles moléculaires, Phylogénie, Polyosides, Structure secondaire des protéines.

English descriptors

KwdEn :
- Animals, Birds (virology), Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Humans, Influenza A Virus, H5N1 Subtype (metabolism), Insecta, Ligands, Models, Molecular, Mutation (genetics), Phylogeny, Polysaccharides (chemistry), Polysaccharides (metabolism), Protein Structure, Secondary, Receptors, Virus (metabolism), Virus Diseases (virology).
MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus, Polysaccharides.
- chemical , genetics : Hemagglutinin Glycoproteins, Influenza Virus.
- genetics : Mutation.
- metabolism : Influenza A Virus, H5N1 Subtype, Polysaccharides, Receptors, Virus.
- virology : Birds, Virus Diseases.
- Animals, Humans, Insecta, Ligands, Models, Molecular, Phylogeny, Protein Structure, Secondary.

Abstract

Adaptation of avian influenza viruses for replication and transmission in the human host is believed to require mutations in the hemagglutinin glycoprotein (HA) which enable binding to human α2-6 sialosides and concomitant reduction in affinity for avian α2-3 linked sialosides. Here, we show by glycan microarray analyses that the two mutations responsible for such specificity changes in 1957 H2N2 and 1968 H3N2 pandemic viruses, when inserted into recombinant HAs or intact viruses of some recent avian H5N1 isolates (clade 2.2), impart such attributes. This propensity to adapt to human receptors is primarily dependent on arginine at position 193 within the receptor binding site, as well as loss of a vicinal glycosylation site. already have Widespread occurrence of these susceptible H5N1 clade 2.2 influenza strains has already occurred in Europe, the Middle East, and Africa. Thus, these avian strains should be considered ‘high-risk’, because of their significantly lower threshold for acquiring human receptor specificity and, therefore, warrant increased surveillance and further study.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2519951

DOI: 10.1016/j.jmb.2008.04.016
PubMed: 18672252
PubMed Central: 2519951

Affiliations:

Links to Exploration step

PMC:2519951

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Birds (virology)</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (chemistry)</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (genetics)</term>
<term>Humans</term>
<term>Influenza A Virus, H5N1 Subtype (metabolism)</term>
<term>Insecta</term>
<term>Ligands</term>
<term>Models, Molecular</term>
<term>Mutation (genetics)</term>
<term>Phylogeny</term>
<term>Polysaccharides (chemistry)</term>
<term>Polysaccharides (metabolism)</term>
<term>Protein Structure, Secondary</term>
<term>Receptors, Virus (metabolism)</term>
<term>Virus Diseases (virology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Glycoprotéine hémagglutinine du virus influenza ()</term>
<term>Glycoprotéine hémagglutinine du virus influenza (génétique)</term>
<term>Humains</term>
<term>Ligands</term>
<term>Maladies virales (virologie)</term>
<term>Modèles moléculaires</term>
<term>Mutation (génétique)</term>
<term>Oiseaux (virologie)</term>
<term>Phylogénie</term>
<term>Polyosides ()</term>
<term>Polyosides (métabolisme)</term>
<term>Récepteurs viraux (métabolisme)</term>
<term>Sous-type H5N1 du virus de la grippe A (métabolisme)</term>
<term>Structure secondaire des protéines</term>
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<term>Polysaccharides</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term>
<term>Mutation</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza A Virus, H5N1 Subtype</term>
<term>Polysaccharides</term>
<term>Receptors, Virus</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Polyosides</term>
<term>Récepteurs viraux</term>
<term>Sous-type H5N1 du virus de la grippe A</term>
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<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Maladies virales</term>
<term>Oiseaux</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Birds</term>
<term>Virus Diseases</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Humans</term>
<term>Insecta</term>
<term>Ligands</term>
<term>Models, Molecular</term>
<term>Phylogeny</term>
<term>Protein Structure, Secondary</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Glycoprotéine hémagglutinine du virus influenza</term>
<term>Humains</term>
<term>Ligands</term>
<term>Modèles moléculaires</term>
<term>Phylogénie</term>
<term>Polyosides</term>
<term>Structure secondaire des protéines</term>
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<front><div type="abstract" xml:lang="en"><p id="P1">Adaptation of avian influenza viruses for replication and transmission in the human host is believed to require mutations in the hemagglutinin glycoprotein (HA) which enable binding to human α2-6 sialosides and concomitant reduction in affinity for avian α2-3 linked sialosides. Here, we show by glycan microarray analyses that the two mutations responsible for such specificity changes in 1957 H2N2 and 1968 H3N2 pandemic viruses, when inserted into recombinant HAs or intact viruses of some recent avian H5N1 isolates (clade 2.2), impart such attributes. This propensity to adapt to human receptors is primarily dependent on arginine at position 193 within the receptor binding site, as well as loss of a vicinal glycosylation site. already have Widespread occurrence of these susceptible H5N1 clade 2.2 influenza strains has already occurred in Europe, the Middle East, and Africa. Thus, these avian strains should be considered ‘high-risk’, because of their significantly lower threshold for acquiring human receptor specificity and, therefore, warrant increased surveillance and further study.</p>
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Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity

Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity

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Descripteurs français

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Abstract

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Links to Exploration step

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