Article: The hemagglutinin structure of an avian H1N1 influenza A virus

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TitleThe hemagglutinin structure of an avian H1N1 influenza A virus
AuthorsLin, T1 2
Wang, G3 4
Li, A1
Zhang, Q1
Wu, C1
Zhang, R1
Cai, Q1
Song, W2
Yuen, KY2
Issue Date2009
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviro
CitationVirology, 2009, v. 392 n. 1, p. 73-81 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.virol.2009.06.028
AbstractThe interaction between hemagglutinin (HA) and receptors is a kernel in the study of evolution and host adaptation of H1N1 influenza A viruses. The notion that the avian HA is associated with preferential specificity for receptors with Siaα2,3Gal glycosidic linkage over those with Siaα2,6Gal linkage is not all consistent with the available data on H1N1 viruses. By x-ray crystallography, the HA structure of an avian H1N1 influenza A virus, as well as its complexes with the receptor analogs, was determined. The structures revealed no preferential binding of avian receptor analogs over that of the human analog, suggesting that the HA/receptor binding might not be as stringent as is commonly believed in determining the host receptor preference for some subtypes of influenza viruses, such as the H1N1 viruses. The structure also showed difference in glycosylation despite the preservation of related sequences, which may partly contribute to the difference between structures of human and avian origin. © 2009 Elsevier Inc. All rights reserved.
ISSN0042-6822
2011 Impact Factor: 3.351
2011 SCImago Journal Rankings: 0.355
DOIhttp://dx.doi.org/10.1016/j.virol.2009.06.028
ISI Accession Number IDWOS:000269783500008
Funding AgencyGrant Number
National Science Foundation of China30870479
111 Project of ChinaB06016
Providence Foundation Limited
Research Fund for Infections Diseases of Hong Kong SAR
Li Ka Shing Foundation
Funding Information:

Discussions with Drs. Yi Guan and Honglin Chen helped greatly on the research, which are gratefully acknowledged. The authors thank the help from Dr. Vukica Srajer and others at the BioCARS of the Advance Photo Sources for data collection and processing. The work is supported by the National Science Foundation of China (Grant No. 30870479), the 111 Project of China No. B06016), the Providence Foundation Limited in memory of the late Dr. Lui Hac Minh, the Research Fund for Infections Diseases of Hong Kong SAR, and the Li Ka Shing Foundation.

ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorLin, T
dc.contributor.authorWang, G
dc.contributor.authorLi, A
dc.contributor.authorZhang, Q
dc.contributor.authorWu, C
dc.contributor.authorZhang, R
dc.contributor.authorCai, Q
dc.contributor.authorSong, W
dc.contributor.authorYuen, KY
dc.date.accessioned2012-08-08T08:51:14Z
dc.date.available2012-08-08T08:51:14Z
dc.date.issued2009
dc.description.abstractThe interaction between hemagglutinin (HA) and receptors is a kernel in the study of evolution and host adaptation of H1N1 influenza A viruses. The notion that the avian HA is associated with preferential specificity for receptors with Siaα2,3Gal glycosidic linkage over those with Siaα2,6Gal linkage is not all consistent with the available data on H1N1 viruses. By x-ray crystallography, the HA structure of an avian H1N1 influenza A virus, as well as its complexes with the receptor analogs, was determined. The structures revealed no preferential binding of avian receptor analogs over that of the human analog, suggesting that the HA/receptor binding might not be as stringent as is commonly believed in determining the host receptor preference for some subtypes of influenza viruses, such as the H1N1 viruses. The structure also showed difference in glycosylation despite the preservation of related sequences, which may partly contribute to the difference between structures of human and avian origin. © 2009 Elsevier Inc. All rights reserved.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationVirology, 2009, v. 392 n. 1, p. 73-81 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.virol.2009.06.028
dc.identifier.citeulike5274256
dc.identifier.doihttp://dx.doi.org/10.1016/j.virol.2009.06.028
dc.identifier.epage81
dc.identifier.isiWOS:000269783500008
Funding AgencyGrant Number
National Science Foundation of China30870479
111 Project of ChinaB06016
Providence Foundation Limited
Research Fund for Infections Diseases of Hong Kong SAR
Li Ka Shing Foundation
Funding Information:

Discussions with Drs. Yi Guan and Honglin Chen helped greatly on the research, which are gratefully acknowledged. The authors thank the help from Dr. Vukica Srajer and others at the BioCARS of the Advance Photo Sources for data collection and processing. The work is supported by the National Science Foundation of China (Grant No. 30870479), the 111 Project of China No. B06016), the Providence Foundation Limited in memory of the late Dr. Lui Hac Minh, the Research Fund for Infections Diseases of Hong Kong SAR, and the Li Ka Shing Foundation.

dc.identifier.issn0042-6822
2011 Impact Factor: 3.351
2011 SCImago Journal Rankings: 0.355
dc.identifier.issue1
dc.identifier.pmid19628241
dc.identifier.scopuseid_2-s2.0-69249221242
dc.identifier.spage73
dc.identifier.urihttp://hdl.handle.net/10722/157556
dc.identifier.volume392
dc.languageeng
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviro
dc.publisher.placeUnited States
dc.relation.ispartofVirology
dc.relation.referencesReferences in Scopus
dc.subject.meshAmino Acid Sequence
dc.subject.meshAnimals
dc.subject.meshBase Sequence
dc.subject.meshBinding Sites
dc.subject.meshBirds - Virology
dc.subject.meshCarbohydrate Sequence
dc.subject.meshCrystallography, X-Ray
dc.subject.meshDna Primers - Genetics
dc.subject.meshGlycosylation
dc.subject.meshHemagglutinin Glycoproteins, Influenza Virus - Chemistry - Genetics
dc.subject.meshHumans
dc.subject.meshInfluenza A Virus, H1n1 Subtype - Chemistry - Genetics
dc.subject.meshMammals
dc.subject.meshModels, Molecular
dc.subject.meshMolecular Sequence Data
dc.subject.meshMolecular Structure
dc.subject.meshProtein Structure, Quaternary
dc.subject.meshReceptors, Virus - Chemistry
dc.subject.meshSequence Homology, Amino Acid
dc.subject.meshSpecies Specificity
dc.subject.meshStatic Electricity
dc.titleThe hemagglutinin structure of an avian H1N1 influenza A virus
dc.typeArticle
Author Affiliations
  1. Xiamen University
  2. Research Centre of Infection and Immunology
  3. Shantou University
  4. Medical College