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2009-06-18Zeitschriftenartikel DOI: 10.1186/1743-422X-6-79
Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein
dc.contributor.authorVoß, Daniel
dc.contributor.authorPfefferle, Susanne
dc.contributor.authorDrosten, Christian
dc.contributor.authorStevermann, Lea
dc.contributor.authorTraggiai, Elisabetta
dc.contributor.authorLanzavecchia, Antonio
dc.contributor.authorBecker, Stephan
dc.date.accessioned2018-05-07T13:23:26Z
dc.date.available2018-05-07T13:23:26Z
dc.date.created2009-11-25
dc.date.issued2009-06-18none
dc.identifier.otherhttp://edoc.rki.de/oa/articles/reGJuFs1aLTQ/PDF/28c8lvWlPkKV2.pdf
dc.identifier.urihttp://edoc.rki.de/176904/481
dc.description.abstractThe glycosylated membrane protein M of the severe acute respiratory syndrome associated coronavirus (SARS-CoV) is the main structural component of the virion and mediates assembly and budding of viral particles. The membrane topology of SARS-CoV M and the functional significance of its N-glycosylation are not completely understood as is its interaction with the surface glycoprotein S. Using biochemical and immunofluorescence analyses we found that M consists of a short glycosylated N-terminal ectodomain, three transmembrane segments and a long, immunogenic C-terminal endodomain. Although the N-glycosylation site of M seems to be highly conserved between group 1 and 3 coronaviruses, studies using a recombinant SARS-CoV expressing a glycosylation-deficient M revealed that N-glycosylation of M neither influence the shape of the virions nor their infectivity in cell culture. Further functional analysis of truncated M proteins showed that the N-terminal 134 amino acids comprising the three transmembrane domains are sufficient to mediate accumulation of M in the Golgi complex and to enforce recruitment of the viral spike protein S to the sites of virus assembly and budding in the ERGIC.eng
dc.language.isoeng
dc.publisherRobert Koch-Institut; Robert Koch-Institut, Infektionskrankheiten / Erreger
dc.subjectVirus Replicationeng
dc.subjectCell Lineeng
dc.subjectHumanseng
dc.subjectAnimalseng
dc.subjectAmino Acid Substitutioneng
dc.subjectCercopithecus aethiopseng
dc.subjectGlycosylationeng
dc.subjectGolgi Apparatus/virologyeng
dc.subjectMembrane Glycoproteins/metabolismeng
dc.subjectMutagenesiseng
dc.subjectSite-Directedeng
dc.subjectSARS Virus/chemistryeng
dc.subjectSARS Virus/physiologyeng
dc.subjectSequence Deletioneng
dc.subjectViral Envelope Proteins/metabolismeng
dc.subjectViral Matrix Proteins/geneticseng
dc.subjectViral Matrix Proteins/metabolismeng
dc.subjectVirus Internalizationeng
dc.subject.ddc610 Medizin
dc.titleStudies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein
dc.typeperiodicalPart
dc.identifier.urnurn:nbn:de:0257-1002903
dc.identifier.doi10.1186/1743-422X-6-79
dc.identifier.doihttp://dx.doi.org/10.25646/406
local.edoc.container-titleVirology Journal
local.edoc.fp-subtypeArtikel
local.edoc.type-nameZeitschriftenartikel
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-urlhttp://www.virologyj.com/content/6/1/79
local.edoc.container-publisher-nameBioMed Central
local.edoc.container-volume6
local.edoc.container-year2009

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