2.50
Hdl Handle:
http://hdl.handle.net/10033/620567
Title:
Caveolin-1 influences human influenza A virus (H1N1) multiplication in cell culture
Authors:
Sun, Lijing; Hemgård, Gun-Viol; Susanto, Sony A; Wirth, Manfred
Abstract:
Abstract Background The threat of recurring influenza pandemics caused by new viral strains and the occurrence of escape mutants necessitate the search for potent therapeutic targets. The dependence of viruses on cellular factors provides a weak-spot in the viral multiplication strategy and a means to interfere with viral multiplication. Results Using a motif-based search strategy for antiviral targets we identified caveolin-1 (Cav-1) as a putative cellular interaction partner of human influenza A viruses, including the pandemic influenza A virus (H1N1) strains of swine origin circulating from spring 2009 on. The influence of Cav-1 on human influenza A/PR/8/34 (H1N1) virus replication was determined in inhibition and competition experiments. RNAi-mediated Cav-1 knock-down as well as transfection of a dominant-negative Cav-1 mutant results in a decrease in virus titre in infected Madin-Darby canine kidney cells (MDCK), a cell line commonly used in basic influenza research as well as in virus vaccine production. To understand the molecular basis of the phenomenon we focussed on the putative caveolin-1 binding domain (CBD) located in the lumenal, juxtamembranal portion of the M2 matrix protein which has been identified in the motif-based search. Pull-down assays and co-immunoprecipitation experiments showed that caveolin-1 binds to M2. The data suggest, that Cav-1 modulates influenza virus A replication presumably based on M2/Cav-1 interaction. Conclusion As Cav-1 is involved in the human influenza A virus life cycle, the multifunctional protein and its interaction with M2 protein of human influenza A viruses represent a promising starting point for the search for antiviral agents.
Citation:
Virology Journal. 2010 May 26;7(1):108
Issue Date:
26-May-2010
URI:
http://dx.doi.org/10.1186/1743-422X-7-108; http://hdl.handle.net/10033/620567
Type:
Journal Article
Appears in Collections:
publications of the research group modell systems for infections and immunity (MSYS)

Full metadata record

DC FieldValue Language
dc.contributor.authorSun, Lijingen
dc.contributor.authorHemgård, Gun-Violen
dc.contributor.authorSusanto, Sony Aen
dc.contributor.authorWirth, Manfreden
dc.date.accessioned2016-11-02T14:46:02Z-
dc.date.available2016-11-02T14:46:02Z-
dc.date.issued2010-05-26en
dc.identifier.citationVirology Journal. 2010 May 26;7(1):108en
dc.identifier.urihttp://dx.doi.org/10.1186/1743-422X-7-108en
dc.identifier.urihttp://hdl.handle.net/10033/620567-
dc.description.abstractAbstract Background The threat of recurring influenza pandemics caused by new viral strains and the occurrence of escape mutants necessitate the search for potent therapeutic targets. The dependence of viruses on cellular factors provides a weak-spot in the viral multiplication strategy and a means to interfere with viral multiplication. Results Using a motif-based search strategy for antiviral targets we identified caveolin-1 (Cav-1) as a putative cellular interaction partner of human influenza A viruses, including the pandemic influenza A virus (H1N1) strains of swine origin circulating from spring 2009 on. The influence of Cav-1 on human influenza A/PR/8/34 (H1N1) virus replication was determined in inhibition and competition experiments. RNAi-mediated Cav-1 knock-down as well as transfection of a dominant-negative Cav-1 mutant results in a decrease in virus titre in infected Madin-Darby canine kidney cells (MDCK), a cell line commonly used in basic influenza research as well as in virus vaccine production. To understand the molecular basis of the phenomenon we focussed on the putative caveolin-1 binding domain (CBD) located in the lumenal, juxtamembranal portion of the M2 matrix protein which has been identified in the motif-based search. Pull-down assays and co-immunoprecipitation experiments showed that caveolin-1 binds to M2. The data suggest, that Cav-1 modulates influenza virus A replication presumably based on M2/Cav-1 interaction. Conclusion As Cav-1 is involved in the human influenza A virus life cycle, the multifunctional protein and its interaction with M2 protein of human influenza A viruses represent a promising starting point for the search for antiviral agents.en
dc.titleCaveolin-1 influences human influenza A virus (H1N1) multiplication in cell cultureen
dc.typeJournal Articleen
dc.language.rfc3066enen
dc.rights.holderSun et al.en
dc.date.updated2015-09-04T08:22:03Zen
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