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Article: Modification of nonstructural protein 1 of influenza a virus by SUMO1

TitleModification of nonstructural protein 1 of influenza a virus by SUMO1
Authors
Issue Date2011
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
Citation
Journal Of Virology, 2011, v. 85 n. 2, p. 1086-1098 How to Cite?
Abstract
Nonstructural protein 1 (NS1) is one of the major factors resulting in the efficient infection rate and high level of virulence of influenza A virus. Although consisting of only approximately 230 amino acids, NS1 has the ability to interfere with several systems of the host viral defense. In the present study, we demonstrate that NS1 of the highly pathogenic avian influenza A/Duck/Hubei/L-1/2004 (H5N1) virus interacts with human Ubc9, which is the E2 conjugating enzyme for sumoylation, and we show that SUMO1 is conjugated to H5N1 NS1 in both transfected and infected cells. Furthermore, two lysine residues in the C terminus of NS1 were identified as SUMO1 acceptor sites. When the SUMO1 acceptor sites were removed by mutation, NS1 underwent rapid degradation. Studies of different influenza A virus strains of human and avian origin showed that the majority of viruses possess an NS1 protein that is modified by SUMO1, except for the recently emerged swine-origin influenza A virus (S-OIV) (H1N1). Interestingly, growth of a sumoylation-deficient WSN virus mutant was retarded compared to that of wild-type virus. Together, these results indicate that sumoylation enhances NS1 stability and thus promotes rapid growth of influenza A virus. Copyright © 2011 American Society for Microbiology. All Rights Reserved.
Persistent Identifierhttp://hdl.handle.net/10722/135280
ISSN
2013 Impact Factor: 4.648
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
European UnionFLUINNATE SP5B-CT-2006-044161
Deutsche ForschungsgemeinschaftSFB 593 TP B1
CASKSCX2-YW-R-161
National Ministry of Science and Technology20072714
National Natural Science Foundation of China30950002
30623003
30721065
30801011
30870126
90713044
Science and Technology Commission of Shanghai Municipality08DZ2291703
088014199
08431903004
National Science and Technology Major Project2008ZX10002-01
2008ZX10004-002
2009ZX10004-105
National 973 Key Project2007CB512404
SPHRFSPHRF2008001
SPHRF2009001
National 863 Project2006AA02A247
Li Kha Shing Foundation
Funding Information:

This work was supported by grants from the European Union (FLUINNATE SP5B-CT-2006-044161), the Deutsche Forschungsgemeinschaft (SFB 593 TP B1), CAS (KSCX2-YW-R-161), the National Ministry of Science and Technology (20072714) and the National Natural Science Foundation of China (30950002, 30623003, 30721065, 30801011, 30870126, and 90713044), the Science and Technology Commission of Shanghai Municipality (08DZ2291703, 088014199, and 08431903004), the National Science and Technology Major Project (2008ZX10002-01, 2008ZX10004-002, and 2009ZX10004-105), the National 973 Key Project (2007CB512404), SPHRF (SPHRF2008001 and SPHRF2009001), the National 863 Project (2006AA02A247), and the Li Kha Shing Foundation.

References

 

DC FieldValueLanguage
dc.contributor.authorXu, Ken_HK
dc.contributor.authorKlenk, Cen_HK
dc.contributor.authorLiu, Ben_HK
dc.contributor.authorKeiner, Ben_HK
dc.contributor.authorCheng, Jen_HK
dc.contributor.authorZheng, BJen_HK
dc.contributor.authorLi, Len_HK
dc.contributor.authorHan, Qen_HK
dc.contributor.authorWang, Cen_HK
dc.contributor.authorLi, Ten_HK
dc.contributor.authorChen, Zen_HK
dc.contributor.authorShu, Yen_HK
dc.contributor.authorLiu, Jen_HK
dc.contributor.authorKlenk, HDen_HK
dc.contributor.authorSun, Ben_HK
dc.date.accessioned2011-07-27T01:31:10Z-
dc.date.available2011-07-27T01:31:10Z-
dc.date.issued2011en_HK
dc.identifier.citationJournal Of Virology, 2011, v. 85 n. 2, p. 1086-1098en_HK
dc.identifier.issn0022-538Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/135280-
dc.description.abstractNonstructural protein 1 (NS1) is one of the major factors resulting in the efficient infection rate and high level of virulence of influenza A virus. Although consisting of only approximately 230 amino acids, NS1 has the ability to interfere with several systems of the host viral defense. In the present study, we demonstrate that NS1 of the highly pathogenic avian influenza A/Duck/Hubei/L-1/2004 (H5N1) virus interacts with human Ubc9, which is the E2 conjugating enzyme for sumoylation, and we show that SUMO1 is conjugated to H5N1 NS1 in both transfected and infected cells. Furthermore, two lysine residues in the C terminus of NS1 were identified as SUMO1 acceptor sites. When the SUMO1 acceptor sites were removed by mutation, NS1 underwent rapid degradation. Studies of different influenza A virus strains of human and avian origin showed that the majority of viruses possess an NS1 protein that is modified by SUMO1, except for the recently emerged swine-origin influenza A virus (S-OIV) (H1N1). Interestingly, growth of a sumoylation-deficient WSN virus mutant was retarded compared to that of wild-type virus. Together, these results indicate that sumoylation enhances NS1 stability and thus promotes rapid growth of influenza A virus. Copyright © 2011 American Society for Microbiology. All Rights Reserved.en_HK
dc.languageengen_US
dc.publisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/en_HK
dc.relation.ispartofJournal of Virologyen_HK
dc.rightsJournal of Virology. Copyright © American Society for Microbiology.-
dc.subject.meshHost-Pathogen Interactions-
dc.subject.meshInfluenza A Virus, H5N1 Subtype - pathogenicity-
dc.subject.meshSUMO-1 Protein - metabolism-
dc.subject.meshUbiquitin-Conjugating Enzymes - metabolism-
dc.subject.meshViral Nonstructural Proteins - genetics - metabolism-
dc.titleModification of nonstructural protein 1 of influenza a virus by SUMO1en_HK
dc.typeArticleen_HK
dc.identifier.emailZheng, BJ:bzheng@hkucc.hku.hken_HK
dc.identifier.authorityZheng, BJ=rp00353en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1128/JVI.00877-10en_HK
dc.identifier.pmid21047957en_HK
dc.identifier.pmcidPMC3020006-
dc.identifier.scopuseid_2-s2.0-78650673299en_HK
dc.identifier.hkuros188638en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-78650673299&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume85en_HK
dc.identifier.issue2en_HK
dc.identifier.spage1086en_HK
dc.identifier.epage1098en_HK
dc.identifier.isiWOS:000285554300043-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridXu, K=7403282210en_HK
dc.identifier.scopusauthoridKlenk, C=25028182100en_HK
dc.identifier.scopusauthoridLiu, B=36079151900en_HK
dc.identifier.scopusauthoridKeiner, B=36054763000en_HK
dc.identifier.scopusauthoridCheng, J=7405940606en_HK
dc.identifier.scopusauthoridZheng, BJ=7201780588en_HK
dc.identifier.scopusauthoridLi, L=36064664900en_HK
dc.identifier.scopusauthoridHan, Q=7202485404en_HK
dc.identifier.scopusauthoridWang, C=35621051600en_HK
dc.identifier.scopusauthoridLi, T=10641226800en_HK
dc.identifier.scopusauthoridChen, Z=7409481304en_HK
dc.identifier.scopusauthoridShu, Y=7103239481en_HK
dc.identifier.scopusauthoridLiu, J=36165045800en_HK
dc.identifier.scopusauthoridKlenk, HD=24432172000en_HK
dc.identifier.scopusauthoridSun, B=24734369900en_HK

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