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

TitleThe hemagglutinin structure of an avian H1N1 influenza A virus
Authors
Issue Date2009
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviro
Citation
Virology, 2009, v. 392 n. 1, p. 73-81 How to Cite?
Abstract
The 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.
Persistent Identifierhttp://hdl.handle.net/10722/157556
ISSN
2013 Impact Factor: 3.278
ISI Accession Number ID
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.

References

 

DC FieldValueLanguage
dc.contributor.authorLin, Ten_US
dc.contributor.authorWang, Gen_US
dc.contributor.authorLi, Aen_US
dc.contributor.authorZhang, Qen_US
dc.contributor.authorWu, Cen_US
dc.contributor.authorZhang, Ren_US
dc.contributor.authorCai, Qen_US
dc.contributor.authorSong, Wen_US
dc.contributor.authorYuen, KYen_US
dc.date.accessioned2012-08-08T08:51:14Z-
dc.date.available2012-08-08T08:51:14Z-
dc.date.issued2009en_US
dc.identifier.citationVirology, 2009, v. 392 n. 1, p. 73-81en_US
dc.identifier.issn0042-6822en_US
dc.identifier.urihttp://hdl.handle.net/10722/157556-
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.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviroen_US
dc.relation.ispartofVirologyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshBirds - Virologyen_US
dc.subject.meshCarbohydrate Sequenceen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshDna Primers - Geneticsen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHemagglutinin Glycoproteins, Influenza Virus - Chemistry - Geneticsen_US
dc.subject.meshHumansen_US
dc.subject.meshInfluenza A Virus, H1n1 Subtype - Chemistry - Geneticsen_US
dc.subject.meshMammalsen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshProtein Structure, Quaternaryen_US
dc.subject.meshReceptors, Virus - Chemistryen_US
dc.subject.meshSequence Homology, Amino Aciden_US
dc.subject.meshSpecies Specificityen_US
dc.subject.meshStatic Electricityen_US
dc.titleThe hemagglutinin structure of an avian H1N1 influenza A virusen_US
dc.typeArticleen_US
dc.identifier.emailYuen, KY:kyyuen@hkucc.hku.hken_US
dc.identifier.authorityYuen, KY=rp00366en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.virol.2009.06.028en_US
dc.identifier.pmid19628241en_US
dc.identifier.scopuseid_2-s2.0-69249221242en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-69249221242&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume392en_US
dc.identifier.issue1en_US
dc.identifier.spage73en_US
dc.identifier.epage81en_US
dc.identifier.isiWOS:000269783500008-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLin, T=7404860987en_US
dc.identifier.scopusauthoridWang, G=35216852000en_US
dc.identifier.scopusauthoridLi, A=55244068500en_US
dc.identifier.scopusauthoridZhang, Q=7406715309en_US
dc.identifier.scopusauthoridWu, C=35216773600en_US
dc.identifier.scopusauthoridZhang, R=24075001700en_US
dc.identifier.scopusauthoridCai, Q=35214536700en_US
dc.identifier.scopusauthoridSong, W=23490429800en_US
dc.identifier.scopusauthoridYuen, KY=36078079100en_US
dc.identifier.citeulike5274256-

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