About: Structural and Functional Bases for Broad-Spectrum Neutralization of Avian and Human Influenza A Viruses

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About: Structural and Functional Bases for Broad-Spectrum Neutralization of Avian and Human Influenza A Viruses Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structural and Functional Bases for Broad-Spectrum Neutralization of Avian and Human Influenza A Viruses
Creator	Sui, Jianhua Aird, Daniel Ali, Maryam Cadwell, Greg Han, Thomas Murakami, Akikazu Perez, Sandra Santelli, Eugenio Stec, Boguslaw Wan, Hongquan Yammanuru, Anuradha Chen, Li-Mei Donis, Ruben Cox, Nancy Bankston, Laurie Hwang, William Liddington, Robert Marasco, Wayne
Source	Medline; PMC
abstract	Influenza virus remains a constant public health threat, owing to its ability to evade immune surveillance through rapid genetic drift and reassortment. Monoclonal antibody (mAb)-based immunotherapy is a promising strategy for disease control. Here we use a human Ab phage display library and H5 hemagglutinin (HA) ectodomain to select ten neutralizing mAbs (nAbs) with a remarkably broad range among Group 1 influenza viruses, including the H5N1 “bird flu” and the H1N1 “Spanish flu” strains. Notably, nine of the Abs utilize the same germline gene, VH1-69. The crystal structure of one mAb bound to H5N1 HA reveals that only the heavy chain inserts into a highly conserved pocket in the HA stem, inhibiting the conformational changes required for membrane fusion. Our studies indicate that nAbs targeting this pocket could provide broad protection against both seasonal and pandemic influenza A infections.
has issue date	2009-02-22(xsd:dateTime)
bibo:doi	10.1038/nsmb.1566
bibo:pmid	19234466
has license	no-cc
sha1sum (hex)	4221d737431125fa7453391cd9922fa236cbcc37
schema:url	https://doi.org/10.1038/nsmb.1566
resource representing a document's title	Structural and Functional Bases for Broad-Spectrum Neutralization of Avian and Human Influenza A Viruses
has PubMed Central identifier	PMC2692245
has PubMed identifier	19234466
schema:publication	Nat Struct Mol Biol
resource representing a document's body	covid:4221d737431125fa7453391cd9922fa236cbcc37#body_text
is schema:about of	named entity 'membrane fusion' named entity 'germline' named entity 'H1N1' named entity 'antibody' named entity 'infection' named entity 'bird flu' named entity 'immune surveillance' named entity 'H5N1' named entity 'Influenza virus' named entity 'ectodomain' named entity 'neutralizing antibodies' named entity 'viruses' named entity 'Spanish flu' named entity 'pandemic influenza viruses' named entity 'VH1' named entity 'heavy chain' named entity 'hemagglutinin' named entity 'phage' named entity 'immunotherapy' named entity 'genetic drift' named entity 'reassortment' named entity 'human influenza' covid:arg/4221d737431125fa7453391cd9922fa236cbcc37 named entity 'influenza viruses' named entity 'crystal structure' named entity 'gene'
is wasQuotedFrom of	covid:arg/4221d737431125fa7453391cd9922fa236cbcc37/0 covid:arg/4221d737431125fa7453391cd9922fa236cbcc37/1
is part of of	Influenza virus remains a constant public health threat, owing to its ability to evade immune surveillance through rapid genetic drift and reassortment. Monoclonal antibody (mAb)-based immunotherapy is a promising strategy for disease control. Here we use a human Ab phage display library and H5 hemagglutinin (HA) ectodomain to select ten neutralizing mAbs (nAbs) with a remarkably broad range among Group 1 influenza viruses, including the H5N1 “bird flu” and the H1N1 “Spanish flu” strains. Notably, nine of the Abs utilize the same germline gene, VH1-69. The crystal structure of one mAb bound to H5N1 HA reveals that only the heavy chain inserts into a highly conserved pocket in the HA stem, inhibiting the conformational changes required for membrane fusion. Our studies indicate that nAbs targeting this pocket could provide broad protection against both seasonal and pandemic influenza A infections. Structural and Functional Bases for Broad-Spectrum Neutralization of Avian and Human Influenza A Viruses covid:4221d737431125fa7453391cd9922fa236cbcc37#body_text

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