H2N2V1, PubMed, Checkpoint, bibRecord, 000121

A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin.

Identifieur interne : 000121 ( PubMed/Checkpoint ); précédent : 000120; suivant : 000122

A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin.

Auteurs : Rui Xu [États-Unis] ; Jens C. Krause ; Ryan Mcbride ; James C. Paulson ; James E. Crowe ; Ian A. Wilson

Source :

Nature structural & molecular biology [ 1545-9985 ] ; 2013.

RBID : pubmed:23396351

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Antibodies, Neutralizing (chemistry), Antibodies, Neutralizing (immunology), Antibodies, Viral (genetics), Antibodies, Viral (immunology), Antigen-Antibody Complex, Binding Sites, Crystallography, X-Ray, Epitopes, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (immunology), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Humans, Immunoglobulin Fab Fragments (chemistry), Immunoglobulin Fab Fragments (immunology), Immunoglobulin Fab Fragments (metabolism), Influenza A Virus, H2N2 Subtype (immunology), Molecular Sequence Data, Mutation, Protein Conformation, Tryptophan (immunology), Tryptophan (metabolism), Tyrosine (metabolism).
MESH :
- chemical , chemistry : Antibodies, Neutralizing, Hemagglutinin Glycoproteins, Influenza Virus, Immunoglobulin Fab Fragments.
- chemical , genetics : Antibodies, Viral.
- chemical , immunology : Antibodies, Neutralizing, Antibodies, Viral, Hemagglutinin Glycoproteins, Influenza Virus, Immunoglobulin Fab Fragments, Tryptophan.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Immunoglobulin Fab Fragments, Tryptophan, Tyrosine.
- immunology : Influenza A Virus, H2N2 Subtype.
- Amino Acid Motifs, Amino Acid Sequence, Antigen-Antibody Complex, Binding Sites, Crystallography, X-Ray, Epitopes, Humans, Molecular Sequence Data, Mutation, Protein Conformation.

Abstract

Influenza virus hemagglutinin (HA) mediates receptor binding and viral entry during influenza infection. The development of receptor analogs as viral-entry blockers has not been successful, which suggests that sialic acid may not be an ideal scaffold to obtain broad, potent HA inhibitors. Here, we report crystal structures of Fab fragments from three human antibodies that neutralize the 1957 pandemic H2N2 influenza virus in complex with H2 HA. All three antibodies use an aromatic residue to plug a conserved cavity in the HA receptor-binding site. Each antibody interacts with the absolutely conserved HA1 Trp153 at the cavity base through π-π stacking with the signature Phe54 of two VH1-69-encoded antibodies or a tyrosine from HCDR3 in the other antibody. This highly conserved interaction can be used as a starting point to design inhibitors targeting this conserved hydrophobic pocket in influenza viruses.

DOI: 10.1038/nsmb.2500
PubMed: 23396351

Affiliations:

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

to stream PubMed, to step Corpus: 000128
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Links to Exploration step

pubmed:23396351

Le document en format XML

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<front><div type="abstract" xml:lang="en">Influenza virus hemagglutinin (HA) mediates receptor binding and viral entry during influenza infection. The development of receptor analogs as viral-entry blockers has not been successful, which suggests that sialic acid may not be an ideal scaffold to obtain broad, potent HA inhibitors. Here, we report crystal structures of Fab fragments from three human antibodies that neutralize the 1957 pandemic H2N2 influenza virus in complex with H2 HA. All three antibodies use an aromatic residue to plug a conserved cavity in the HA receptor-binding site. Each antibody interacts with the absolutely conserved HA1 Trp153 at the cavity base through π-π stacking with the signature Phe54 of two VH1-69-encoded antibodies or a tyrosine from HCDR3 in the other antibody. This highly conserved interaction can be used as a starting point to design inhibitors targeting this conserved hydrophobic pocket in influenza viruses.</div>
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A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin.

A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin.

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