PandemieGrippaleV1, PubMed, Curation, bibRecord, 001E41

A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity.

Identifieur interne : 001E41 ( PubMed/Curation ); précédent : 001E40; suivant : 001E42

A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity.

Auteurs : Laurel Glaser [États-Unis] ; James Stevens ; Dmitriy Zamarin ; Ian A. Wilson ; Adolfo García-Sastre ; Terrence M. Tumpey ; Christopher F. Basler ; Jeffery K. Taubenberger ; Peter Palese

Source :

Journal of virology [ 0022-538X ] ; 2005.

RBID : pubmed:16103207

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Substitution, Animals, Chickens, Erythrocytes, Hemagglutination Tests, Hemagglutinin Glycoproteins, Influenza Virus (genetics), Hemagglutinin Glycoproteins, Influenza Virus (immunology), N-Acetylneuraminic Acid (chemistry), Orthomyxoviridae (genetics), Orthomyxoviridae (immunology), Orthomyxoviridae Infections (virology), Receptors, Virus (chemistry), Receptors, Virus (immunology), Species Specificity.
MESH :
- chemical , chemistry : N-Acetylneuraminic Acid, Receptors, Virus.
- chemical , genetics : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , immunology : Hemagglutinin Glycoproteins, Influenza Virus, Receptors, Virus.
- genetics : Orthomyxoviridae.
- immunology : Orthomyxoviridae.
- virology : Orthomyxoviridae Infections.
- Amino Acid Substitution, Animals, Chickens, Erythrocytes, Hemagglutination Tests, Species Specificity.

Abstract

The receptor binding specificity of influenza viruses may be important for host restriction of human and avian viruses. Here, we show that the hemagglutinin (HA) of the virus that caused the 1918 influenza pandemic has strain-specific differences in its receptor binding specificity. The A/South Carolina/1/18 HA preferentially binds the alpha2,6 sialic acid (human) cellular receptor, whereas the A/New York/1/18 HA, which differs by only one amino acid, binds both the alpha2,6 and the alpha2,3 sialic acid (avian) cellular receptors. Compared to the conserved consensus sequence in the receptor binding site of avian HAs, only a single amino acid at position 190 was changed in the A/New York/1/18 HA. Mutation of this single amino acid back to the avian consensus resulted in a preference for the avian receptor.

DOI: 10.1128/JVI.79.17.11533-11536.2005
PubMed: 16103207

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The receptor binding specificity of influenza viruses may be important for host restriction of human and avian viruses. Here, we show that the hemagglutinin (HA) of the virus that caused the 1918 influenza pandemic has strain-specific differences in its receptor binding specificity. The A/South Carolina/1/18 HA preferentially binds the alpha2,6 sialic acid (human) cellular receptor, whereas the A/New York/1/18 HA, which differs by only one amino acid, binds both the alpha2,6 and the alpha2,3 sialic acid (avian) cellular receptors. Compared to the conserved consensus sequence in the receptor binding site of avian HAs, only a single amino acid at position 190 was changed in the A/New York/1/18 HA. Mutation of this single amino acid back to the avian consensus resulted in a preference for the avian receptor.</div>
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<Abstract><AbstractText>The receptor binding specificity of influenza viruses may be important for host restriction of human and avian viruses. Here, we show that the hemagglutinin (HA) of the virus that caused the 1918 influenza pandemic has strain-specific differences in its receptor binding specificity. The A/South Carolina/1/18 HA preferentially binds the alpha2,6 sialic acid (human) cellular receptor, whereas the A/New York/1/18 HA, which differs by only one amino acid, binds both the alpha2,6 and the alpha2,3 sialic acid (avian) cellular receptors. Compared to the conserved consensus sequence in the receptor binding site of avian HAs, only a single amino acid at position 190 was changed in the A/New York/1/18 HA. Mutation of this single amino acid back to the avian consensus resulted in a preference for the avian receptor.</AbstractText>
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<Reference><Citation>Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1651-6</Citation>
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   |texte=   A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity.
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A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity.

A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity.

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