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Article: The role of the N-terminal caspase cleavage site in the nucleoprotein of influenza A virus in vitro and in vivo

TitleThe role of the N-terminal caspase cleavage site in the nucleoprotein of influenza A virus in vitro and in vivo
Authors
Issue Date2008
PublisherSpringer Wien. The Journal's web site is located at http://www.springer.com/springerwiennewyork/medicine/journal/705
Citation
Archives Of Virology, 2008, v. 153 n. 3, p. 427-434 How to Cite?
AbstractThe N-terminal caspase cleavage in the nucleoprotein (NP) of influenza A virus is correlated with the host origin of the virus, thus could be a molecular determinant for host range. We studied how mutations targeting the NP cleavage motif of human and avian influenza viruses affect virus replication in vitro and in vivo. The "avian-like" D16→G substitution in the NP, which makes this protein resistant to cleavage, did not significantly affect the human A/Puerto Rico/8/34 (H1N1) virus replication in vitro but decreased the lethality of this virus in mice by 68-fold. Gene incompatibility contributed to the attenuated phenotype of the reassortant A/Puerto Rico/8/34 virus with avian NP derived from A/Teal/Hong Kong/w312/97 (H6N1) virus in vitro and in vivo. Insertion of the "human-like" G16→D mutation into avian NP, which resulted in susceptibility to caspase cleavage, did not rescue virulence, but made the reassortant virus even more attenuated. Introducing the human-like G16→D substitution into the NP of highly pathogenic A/Vietnam/1203/04 (H5N1) virus decreased lethality in mice. We confirmed that position 16, which associated with the N-terminal caspase cleavage of the NP, is important for optimal virus fitness in vitro and in vivo. An avian-like mutation at position 16 in the NP of human virus as well as a human-like substitution at this residue in avian NP both resulted in virus attenuation. © 2007 Springer-Verlag.
Persistent Identifierhttp://hdl.handle.net/10722/179808
ISSN
2015 Impact Factor: 2.255
2015 SCImago Journal Rankings: 1.086
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLipatov, ASen_US
dc.contributor.authorYen, HLen_US
dc.contributor.authorSalomon, Ren_US
dc.contributor.authorOzaki, Hen_US
dc.contributor.authorHoffmann, Een_US
dc.contributor.authorWebster, RGen_US
dc.date.accessioned2012-12-19T10:05:00Z-
dc.date.available2012-12-19T10:05:00Z-
dc.date.issued2008en_US
dc.identifier.citationArchives Of Virology, 2008, v. 153 n. 3, p. 427-434en_US
dc.identifier.issn0304-8608en_US
dc.identifier.urihttp://hdl.handle.net/10722/179808-
dc.description.abstractThe N-terminal caspase cleavage in the nucleoprotein (NP) of influenza A virus is correlated with the host origin of the virus, thus could be a molecular determinant for host range. We studied how mutations targeting the NP cleavage motif of human and avian influenza viruses affect virus replication in vitro and in vivo. The "avian-like" D16→G substitution in the NP, which makes this protein resistant to cleavage, did not significantly affect the human A/Puerto Rico/8/34 (H1N1) virus replication in vitro but decreased the lethality of this virus in mice by 68-fold. Gene incompatibility contributed to the attenuated phenotype of the reassortant A/Puerto Rico/8/34 virus with avian NP derived from A/Teal/Hong Kong/w312/97 (H6N1) virus in vitro and in vivo. Insertion of the "human-like" G16→D mutation into avian NP, which resulted in susceptibility to caspase cleavage, did not rescue virulence, but made the reassortant virus even more attenuated. Introducing the human-like G16→D substitution into the NP of highly pathogenic A/Vietnam/1203/04 (H5N1) virus decreased lethality in mice. We confirmed that position 16, which associated with the N-terminal caspase cleavage of the NP, is important for optimal virus fitness in vitro and in vivo. An avian-like mutation at position 16 in the NP of human virus as well as a human-like substitution at this residue in avian NP both resulted in virus attenuation. © 2007 Springer-Verlag.en_US
dc.languageengen_US
dc.publisherSpringer Wien. The Journal's web site is located at http://www.springer.com/springerwiennewyork/medicine/journal/705en_US
dc.relation.ispartofArchives of Virologyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCaspases - Metabolismen_US
dc.subject.meshChickens - Virologyen_US
dc.subject.meshHumansen_US
dc.subject.meshInfluenza A Virus - Genetics - Pathogenicity - Physiologyen_US
dc.subject.meshInfluenza In Birds - Virologyen_US
dc.subject.meshInfluenza, Human - Virologyen_US
dc.subject.meshMiceen_US
dc.subject.meshMutationen_US
dc.subject.meshNucleoproteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshRna-Binding Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshRecombination, Geneticen_US
dc.subject.meshViral Core Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshVirus Replication - Geneticsen_US
dc.titleThe role of the N-terminal caspase cleavage site in the nucleoprotein of influenza A virus in vitro and in vivoen_US
dc.typeArticleen_US
dc.identifier.emailYen, HL: hyen@hku.hken_US
dc.identifier.authorityYen, HL=rp00304en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s00705-007-0003-8en_US
dc.identifier.pmid18058063-
dc.identifier.scopuseid_2-s2.0-39749184051en_US
dc.identifier.volume153en_US
dc.identifier.issue3en_US
dc.identifier.spage427en_US
dc.identifier.epage434en_US
dc.identifier.isiWOS:000253525300004-
dc.publisher.placeAustriaen_US
dc.identifier.scopusauthoridLipatov, AS=7005117347en_US
dc.identifier.scopusauthoridYen, HL=7102476668en_US
dc.identifier.scopusauthoridSalomon, R=12786463900en_US
dc.identifier.scopusauthoridOzaki, H=7201753697en_US
dc.identifier.scopusauthoridHoffmann, E=7201369718en_US
dc.identifier.scopusauthoridWebster, RG=36048363100en_US

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