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, B1 3 4
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
2011 Impact Factor: 5.402
2011 SCImago Journal Rankings: 0.745
DOIhttp://dx.doi.org/10.1128/JVI.06003-11
PubMed Central IDPMC3264383
ReferencesReferences in Scopus
DC Field
Value
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.
dc.description.naturelink_to_OA_fulltext
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
dc.identifier.epage1801
dc.identifier.hkuros203742
dc.identifier.issn0022-538X
2011 Impact Factor: 5.402
2011 SCImago Journal Rankings: 0.745
dc.identifier.issue3
dc.identifier.openurl
dc.identifier.pmcidPMC3264383
dc.identifier.pmid22114333
dc.identifier.scopuseid_2-s2.0-84863158307
dc.identifier.spage1789
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
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