Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic.
Identifieur interne : 000214 ( PubMed/Corpus ); précédent : 000213; suivant : 000215Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic.
Auteurs : Rui Xu ; Ryan Mcbride ; James C. Paulson ; Christopher F. Basler ; Ian A. WilsonSource :
- Journal of virology [ 1098-5514 ] ; 2010.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antigens, Viral (chemistry), Antigens, Viral (genetics), Antigens, Viral (history), Birds, Crystallography, X-Ray, Disease Outbreaks (history), Evolution, Molecular, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Hemagglutinin Glycoproteins, Influenza Virus (history), Hemagglutinin Glycoproteins, Influenza Virus (immunology), History, 20th Century, Humans, Influenza A Virus, H2N2 Subtype (chemistry), Influenza A Virus, H2N2 Subtype (genetics), Influenza A Virus, H2N2 Subtype (immunology), Influenza A Virus, H2N2 Subtype (pathogenicity), Influenza in Birds (history), Influenza in Birds (virology), Influenza, Human (epidemiology), Influenza, Human (history), Influenza, Human (virology), Models, Molecular, Molecular Sequence Data, Orthomyxoviridae Infections (history), Orthomyxoviridae Infections (veterinary), Orthomyxoviridae Infections (virology), Receptors, Virus (physiology), Sequence Homology, Amino Acid, Species Specificity, Swine, Zoonoses (history), Zoonoses (virology).
- MESH :
- chemical , chemistry : Antigens, Viral, Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , genetics : Antigens, Viral, Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , history : Antigens, Viral, Hemagglutinin Glycoproteins, Influenza Virus.
- chemistry : Influenza A Virus, H2N2 Subtype.
- epidemiology : Influenza, Human.
- genetics : Influenza A Virus, H2N2 Subtype.
- history : Disease Outbreaks, Influenza in Birds, Influenza, Human, Orthomyxoviridae Infections, Zoonoses.
- chemical , immunology : Hemagglutinin Glycoproteins, Influenza Virus, Influenza A Virus, H2N2 Subtype.
- pathogenicity : Influenza A Virus, H2N2 Subtype.
- chemical , physiology : Receptors, Virus.
- veterinary : Orthomyxoviridae Infections.
- virology : Influenza in Birds, Influenza, Human, Orthomyxoviridae Infections, Zoonoses.
- Amino Acid Sequence, Animals, Birds, Crystallography, X-Ray, Evolution, Molecular, History, 20th Century, Humans, Models, Molecular, Molecular Sequence Data, Sequence Homology, Amino Acid, Species Specificity, Swine.
Abstract
The hemagglutinin (HA) envelope protein of influenza viruses mediates essential viral functions, including receptor binding and membrane fusion, and is the major viral antigen for antibody neutralization. The 1957 H2N2 subtype (Asian flu) was one of the three great influenza pandemics of the last century and caused 1 million deaths globally from 1957 to 1968. Three crystal structures of 1957 H2 HAs have been determined at 1.60 to 1.75 A resolutions to investigate the structural basis for their antigenicity and evolution from avian to human binding specificity that contributed to its introduction into the human population. These structures, which represent the highest resolutions yet recorded for a complete ectodomain of a glycosylated viral surface antigen, along with the results of glycan microarray binding analysis, suggest that a hydrophobicity switch at residue 226 and elongation of receptor-binding sites were both critical for avian H2 HA to acquire human receptor specificity. H2 influenza viruses continue to circulate in birds and pigs and, therefore, remain a substantial threat for transmission to humans. The H2 HA structure also reveals a highly conserved epitope that could be harnessed in the design of a broader and more universal influenza A virus vaccine.
DOI: 10.1128/JVI.02162-09
PubMed: 20007271
Links to Exploration step
pubmed:20007271Le document en format XML
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The 1957 H2N2 subtype (Asian flu) was one of the three great influenza pandemics of the last century and caused 1 million deaths globally from 1957 to 1968. Three crystal structures of 1957 H2 HAs have been determined at 1.60 to 1.75 A resolutions to investigate the structural basis for their antigenicity and evolution from avian to human binding specificity that contributed to its introduction into the human population. These structures, which represent the highest resolutions yet recorded for a complete ectodomain of a glycosylated viral surface antigen, along with the results of glycan microarray binding analysis, suggest that a hydrophobicity switch at residue 226 and elongation of receptor-binding sites were both critical for avian H2 HA to acquire human receptor specificity. H2 influenza viruses continue to circulate in birds and pigs and, therefore, remain a substantial threat for transmission to humans. The H2 HA structure also reveals a highly conserved epitope that could be harnessed in the design of a broader and more universal influenza A virus vaccine.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20007271</PMID><DateCompleted><Year>2010</Year><Month>02</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>84</Volume><Issue>4</Issue><PubDate><Year>2010</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic.</ArticleTitle><Pagination><MedlinePgn>1715-21</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.02162-09</ELocationID><Abstract><AbstractText>The hemagglutinin (HA) envelope protein of influenza viruses mediates essential viral functions, including receptor binding and membrane fusion, and is the major viral antigen for antibody neutralization. The 1957 H2N2 subtype (Asian flu) was one of the three great influenza pandemics of the last century and caused 1 million deaths globally from 1957 to 1968. Three crystal structures of 1957 H2 HAs have been determined at 1.60 to 1.75 A resolutions to investigate the structural basis for their antigenicity and evolution from avian to human binding specificity that contributed to its introduction into the human population. These structures, which represent the highest resolutions yet recorded for a complete ectodomain of a glycosylated viral surface antigen, along with the results of glycan microarray binding analysis, suggest that a hydrophobicity switch at residue 226 and elongation of receptor-binding sites were both critical for avian H2 HA to acquire human receptor specificity. H2 influenza viruses continue to circulate in birds and pigs and, therefore, remain a substantial threat for transmission to humans. The H2 HA structure also reveals a highly conserved epitope that could be harnessed in the design of a broader and more universal influenza A virus vaccine.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Rui</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Molecular Biology, BCC-206, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>McBride</LastName><ForeName>Ryan</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Paulson</LastName><ForeName>James C</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Basler</LastName><ForeName>Christopher F</ForeName><Initials>CF</Initials></Author><Author ValidYN="Y"><LastName>Wilson</LastName><ForeName>Ian A</ForeName><Initials>IA</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P01 AI058113</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U54 GM062116</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI058113</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM62116</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016456">Historical Article</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate 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Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 000214 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:20007271
|texte= Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:20007271" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a H2N2V1
| This area was generated with Dilib version V0.6.33. |  |