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Article: Modification of nonstructural protein 1 of influenza a virus by SUMO1
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TitleModification of nonstructural protein 1 of influenza a virus by SUMO1
 
AuthorsXu, K8
Klenk, C3
Liu, B2
Keiner, B7
Cheng, J2
Zheng, BJ1
Li, L8
Han, Q8
Wang, C6
Li, T10
Chen, Z5
Shu, Y4
Liu, J9
Klenk, HD7
Sun, B8 6
 
Issue Date2011
 
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
 
CitationJournal Of Virology, 2011, v. 85 n. 2, p. 1086-1098 [How to Cite?]
DOI: http://dx.doi.org/10.1128/JVI.00877-10
 
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.
 
ISSN0022-538X
2012 Impact Factor: 5.076
2012 SCImago Journal Rankings: 2.559
 
DOIhttp://dx.doi.org/10.1128/JVI.00877-10
 
PubMed Central IDPMC3020006
 
ISI Accession Number IDWOS:000285554300043
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.

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorXu, K
 
dc.contributor.authorKlenk, C
 
dc.contributor.authorLiu, B
 
dc.contributor.authorKeiner, B
 
dc.contributor.authorCheng, J
 
dc.contributor.authorZheng, BJ
 
dc.contributor.authorLi, L
 
dc.contributor.authorHan, Q
 
dc.contributor.authorWang, C
 
dc.contributor.authorLi, T
 
dc.contributor.authorChen, Z
 
dc.contributor.authorShu, Y
 
dc.contributor.authorLiu, J
 
dc.contributor.authorKlenk, HD
 
dc.contributor.authorSun, B
 
dc.date.accessioned2011-07-27T01:31:10Z
 
dc.date.available2011-07-27T01:31:10Z
 
dc.date.issued2011
 
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.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationJournal Of Virology, 2011, v. 85 n. 2, p. 1086-1098 [How to Cite?]
DOI: http://dx.doi.org/10.1128/JVI.00877-10
 
dc.identifier.doihttp://dx.doi.org/10.1128/JVI.00877-10
 
dc.identifier.epage1098
 
dc.identifier.hkuros188638
 
dc.identifier.isiWOS:000285554300043
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.

 
dc.identifier.issn0022-538X
2012 Impact Factor: 5.076
2012 SCImago Journal Rankings: 2.559
 
dc.identifier.issue2
 
dc.identifier.pmcidPMC3020006
 
dc.identifier.pmid21047957
 
dc.identifier.scopuseid_2-s2.0-78650673299
 
dc.identifier.spage1086
 
dc.identifier.urihttp://hdl.handle.net/10722/135280
 
dc.identifier.volume85
 
dc.languageeng
 
dc.publisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
 
dc.publisher.placeUnited States
 
dc.relation.ispartofJournal of Virology
 
dc.relation.referencesReferences in Scopus
 
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 SUMO1
 
dc.typeArticle
 
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<contributor.author>Keiner, B</contributor.author>
<contributor.author>Cheng, J</contributor.author>
<contributor.author>Zheng, BJ</contributor.author>
<contributor.author>Li, L</contributor.author>
<contributor.author>Han, Q</contributor.author>
<contributor.author>Wang, C</contributor.author>
<contributor.author>Li, T</contributor.author>
<contributor.author>Chen, Z</contributor.author>
<contributor.author>Shu, Y</contributor.author>
<contributor.author>Liu, J</contributor.author>
<contributor.author>Klenk, HD</contributor.author>
<contributor.author>Sun, B</contributor.author>
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<description.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 &#169; 2011 American Society for Microbiology. All Rights Reserved.</description.abstract>
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Author Affiliations
  1. The University of Hong Kong
  2. Shanghai Jiaotong University
  3. Julius-Maximilians-Universität Würzburg
  4. Chinese Center for Disease Control and Prevention
  5. Shanghai Institute of Biological Products
  6. Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Sciences Chinese Academy of Sciences
  7. Universität Marburg
  8. Chinese Academy of Sciences
  9. China Agricultural University
  10. Wuhan Institute of Virology Chinese Academy of Sciences