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2011-10-19Zeitschriftenartikel DOI: 10.1099/vir.0.038554-0
Growth of influenza A virus is not impeded by simultaneous removal of the cholesterol binding and acylation sites in the M2 protein
dc.contributor.authorThaa, Bastian
dc.contributor.authorTielesch, Claudia
dc.contributor.authorMöller, Lars
dc.contributor.authorSchmitt, Armin O.
dc.contributor.authorWolff, Thorsten
dc.contributor.authorBannert, Norbert
dc.contributor.authorHerrmann, Andreas
dc.contributor.authorVeit, Michael
dc.date.accessioned2018-05-07T16:01:04Z
dc.date.available2018-05-07T16:01:04Z
dc.date.created2012-11-05
dc.date.issued2011-10-19none
dc.identifier.otherhttp://edoc.rki.de/oa/articles/repgXmLPCz8JY/PDF/26WQuGGfAweAM.pdf
dc.identifier.urihttp://edoc.rki.de/176904/1337
dc.description.abstractInfluenza virus assembly and budding occur in the 'budozone', a coalesced raft domain in the plasma membrane. The viral transmembrane protein M2 is implicated in virus particle scission, the ultimate step in virus budding, probably by wedge-like insertion of an amphiphilic helix into the membrane. In order to do this, M2 is hypothesized to be targeted to the edge of the budozone, mediated by acylation and cholesterol binding. It was recently shown that acylation and cholesterol binding affect the membrane association of the cytoplasmic tail of M2 and targeting of the protein to coalesced rafts. This study tested whether combined removal of the acylation site (C50) and the cholesterol recognition/interaction amino acid consensus motifs (key residues Y52 and Y57) in the amphiphilic helix of M2 influenced virus formation. Recombinant influenza viruses were generated in the influenza strain A/WSN/33 background with mutations in one or both of these features. In comparison with the wild-type, all mutant viruses showed very similar growth kinetics in various cell types. Wild-type and mutant viruses differed in their relative M2 content but not regarding the major structural proteins. The morphology of the viruses was not affected by mutating M2. Moreover, wild-type and mutant viruses showed comparable competitive fitness in infected cells. Lastly, a global comparison of M2 sequences revealed that there are natural virus strains with M2 devoid of both lipid-association motifs. Taken together, these results indicate that the acylation and cholesterol-binding motifs in M2 are not crucial for the replication of influenza virus in cell culture, indicating that other factors can target M2 to the budding site.eng
dc.language.isoeng
dc.publisherRobert Koch-Institut
dc.subjectCell Lineeng
dc.subjectHumanseng
dc.subjectAnimalseng
dc.subjectViral Loadeng
dc.subjectViral Matrix Proteins/metabolismeng
dc.subjectSequence Deletioneng
dc.subjectInfluenza A virus/growth & developmenteng
dc.subjectModels Moleculareng
dc.subjectVirion/ultrastructureeng
dc.subjectVirus Releaseeng
dc.subjectInfluenza A virus/geneticseng
dc.subjectInfluenza A virus/physiologyeng
dc.subjectMicroscopy Electroneng
dc.subjectProtein Processing Post-Translationaleng
dc.subjectAcylationeng
dc.subjectBinding Siteseng
dc.subjectCholesterol/metabolismeng
dc.subjectInfluenza A virus/ultrastructureeng
dc.subjectMutant Proteins/chemistryeng
dc.subjectMutant Proteins/geneticseng
dc.subjectMutant Proteins/metabolismeng
dc.subjectViral Matrix Proteins/chemistryeng
dc.subjectViral Matrix Proteins/genetics*eng
dc.subjectViral Plaque Assayeng
dc.subject.ddc610 Medizin
dc.titleGrowth of influenza A virus is not impeded by simultaneous removal of the cholesterol binding and acylation sites in the M2 protein
dc.typeperiodicalPart
dc.identifier.urnurn:nbn:de:0257-10027681
dc.identifier.doi10.1099/vir.0.038554-0
dc.identifier.doihttp://dx.doi.org/10.25646/1262
local.edoc.container-titleJournal of General Virology
local.edoc.container-textThaa, B., Tielesch, C., Möller, L., Schmitt, A.O., Wolff, T., Bannert, N., Herrmann, A., Veit, M. Growth of influenza A virus is not impeded by simultaneous removal of the cholesterol-binding and acylation sites in the M2 protein (2012) Journal of General Virology, 93 (2), pp. 282-292.
local.edoc.fp-subtypeArtikel
local.edoc.type-nameZeitschriftenartikel
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-urlhttp://vir.sgmjournals.org/content/early/2011/10/13/vir.0.038554-0
local.edoc.container-publisher-nameSociety for General Microbiology
local.edoc.container-volume93
local.edoc.container-issue2
local.edoc.container-year2012

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