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Article: Human annexin A6 interacts with influenza a virus protein M2 and negatively modulates infection
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TitleHuman annexin A6 interacts with influenza a virus protein M2 and negatively modulates infection
 
AuthorsMa, H2 4
Kien, F4
Manière, M4
Zhang, Y1 4
Lagarde, N4
Tse, KS4
Poon, LLM2
Nal, B4 3 1
 
Issue Date2012
 
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
 
CitationJournal Of Virology, 2012, v. 86 n. 3, p. 1789-1801 [How to Cite?]
DOI: http://dx.doi.org/10.1128/JVI.06003-11
 
AbstractThe influenza A virus M2 ion channel protein has the longest cytoplasmic tail (CT) among the three viral envelope proteins and is well conserved between different viral strains. It is accessible to the host cellular machinery after fusion with the endosomal membrane and during the trafficking, assembly, and budding processes. We hypothesized that identification of host cellular interactants of M2 CT could help us to better understand the molecular mechanisms regulating the M2-dependent stages of the virus life cycle. Using yeast two-hybrid screening with M2 CT as bait, a novel interaction with the human annexin A6 (AnxA6) protein was identified, and their physical interaction was confirmed by coimmunoprecipitation assay and a colocalization study of virus-infected human cells. We found that small interfering RNA (siRNA)-mediated knockdown of AnxA6 expression significantly increased virus production, while its overexpression could reduce the titer of virus progeny, suggesting a negative regulatory role for AnxA6 during influenza A virus infection. Further characterization revealed that AnxA6 depletion or overexpression had no effect on the early stages of the virus life cycle or on viral RNA replication but impaired the release of progeny virus, as suggested by delayed or defective budding events observed at the plasma membrane of virus-infected cells by transmission electron microscopy. Collectively, this work identifies AnxA6 as a novel cellular regulator that targets and impairs the virus budding and release stages of the influenza A virus life cycle. © 2012, American Society for Microbiology.
 
ISSN0022-538X
2012 Impact Factor: 5.076
2012 SCImago Journal Rankings: 2.559
 
DOIhttp://dx.doi.org/10.1128/JVI.06003-11
 
PubMed Central IDPMC3264383
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorMa, H
 
dc.contributor.authorKien, F
 
dc.contributor.authorManière, M
 
dc.contributor.authorZhang, Y
 
dc.contributor.authorLagarde, N
 
dc.contributor.authorTse, KS
 
dc.contributor.authorPoon, LLM
 
dc.contributor.authorNal, B
 
dc.date.accessioned2012-08-16T06:39:38Z
 
dc.date.available2012-08-16T06:39:38Z
 
dc.date.issued2012
 
dc.description.abstractThe influenza A virus M2 ion channel protein has the longest cytoplasmic tail (CT) among the three viral envelope proteins and is well conserved between different viral strains. It is accessible to the host cellular machinery after fusion with the endosomal membrane and during the trafficking, assembly, and budding processes. We hypothesized that identification of host cellular interactants of M2 CT could help us to better understand the molecular mechanisms regulating the M2-dependent stages of the virus life cycle. Using yeast two-hybrid screening with M2 CT as bait, a novel interaction with the human annexin A6 (AnxA6) protein was identified, and their physical interaction was confirmed by coimmunoprecipitation assay and a colocalization study of virus-infected human cells. We found that small interfering RNA (siRNA)-mediated knockdown of AnxA6 expression significantly increased virus production, while its overexpression could reduce the titer of virus progeny, suggesting a negative regulatory role for AnxA6 during influenza A virus infection. Further characterization revealed that AnxA6 depletion or overexpression had no effect on the early stages of the virus life cycle or on viral RNA replication but impaired the release of progeny virus, as suggested by delayed or defective budding events observed at the plasma membrane of virus-infected cells by transmission electron microscopy. Collectively, this work identifies AnxA6 as a novel cellular regulator that targets and impairs the virus budding and release stages of the influenza A virus life cycle. © 2012, American Society for Microbiology.
 
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dc.identifier.citationJournal Of Virology, 2012, v. 86 n. 3, p. 1789-1801 [How to Cite?]
DOI: http://dx.doi.org/10.1128/JVI.06003-11
 
dc.identifier.citeulike10252092
 
dc.identifier.doihttp://dx.doi.org/10.1128/JVI.06003-11
 
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2012 SCImago Journal Rankings: 2.559
 
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dc.identifier.pmcidPMC3264383
 
dc.identifier.pmid22114333
 
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dc.identifier.urihttp://hdl.handle.net/10722/161157
 
dc.identifier.volume86
 
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.titleHuman annexin A6 interacts with influenza a virus protein M2 and negatively modulates infection
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong Li Ka Shing Faculty of Medicine
  2. The University of Hong Kong
  3. Brunel University
  4. HKU-Pasteur Research Centre