Pöhlmann, Stefan

[["dc.bibliographiccitation.artnumber","e0189073"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS One"],["dc.bibliographiccitation.lastpage","19"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Brinkmann, Constantin"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Lübke, Anastasia"],["dc.contributor.author","Nehlmeier, Inga"],["dc.contributor.author","Krämer-Kühl, Annika"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2018-11-16T10:48:50Z"],["dc.date.accessioned","2021-10-27T13:13:15Z"],["dc.date.available","2018-11-16T10:48:50Z"],["dc.date.available","2021-10-27T13:13:15Z"],["dc.date.issued","2017"],["dc.description.abstract","Vesicular stomatitis virus (VSV) release from infected cells is inhibited by the interferon (IFN)-inducible antiviral host cell factor tetherin (BST-2, CD317). However, several viruses encode tetherin antagonists and it is at present unknown whether residual VSV spread in tetherin-positive cells is also promoted by a virus-encoded tetherin antagonist. Here, we show that the viral glycoprotein (VSV-G) antagonizes tetherin in transfected cells, although with reduced efficiency as compared to the HIV-1 Vpu protein. Tetherin antagonism did not involve alteration of tetherin expression and was partially dependent on a GXXXG motif in the transmembrane domain of VSV-G. However, mutation of the GXXXG motif did not modulate tetherin sensitivity of infectious VSV. These results identify VSV-G as a tetherin antagonist in transfected cells but fail to provide evidence for a contribution of tetherin antagonism to viral spread."],["dc.identifier.doi","10.1371/journal.pone.0189073"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15673"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91764"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.issn","1932-6203"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The glycoprotein of vesicular stomatitis virus promotes release of virus-like particles from tetherin-positive cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0176597"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Zmora, Pawel"],["dc.contributor.author","Molau-Blazejewska, Paulina"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Walendy-Gnirß, Kerstin"],["dc.contributor.author","Nehlmeier, Inga"],["dc.contributor.author","Hartleib, Anika"],["dc.contributor.author","Moldenhauer, Anna-Sophie"],["dc.contributor.author","Konzok, Sebastian"],["dc.contributor.author","Dehmel, Susann"],["dc.contributor.author","Sewald, Katherina"],["dc.contributor.author","Brinkmann, Constantin"],["dc.contributor.author","Curths, Christoph"],["dc.contributor.author","Knauf, Sascha"],["dc.contributor.author","Gruber, Jens"],["dc.contributor.author","Mätz-Rensing, Kerstin"],["dc.contributor.author","Dahlmann, Franziska"],["dc.contributor.author","Braun, Armin"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2019-07-09T11:43:23Z"],["dc.date.available","2019-07-09T11:43:23Z"],["dc.date.issued","2017"],["dc.description.abstract","The cellular serine protease TMPRSS2, a member of the type II transmembrane serine protease (TTSP) family, cleaves and activates the hemagglutinin of influenza A viruses (FLUAV) in cell culture and is essential for spread of diverse FLUAV in mice. Non-human primates (NHP), in particular rhesus and cynomolgus macaques, serve as animal models for influenza and experimental FLUAV infection of common marmosets has recently also been reported. However, it is currently unknown whether the NHP orthologues of human TMPRSS2 cleave and activate FLUAV hemagglutinin and contribute to viral spread in respiratory tissue. Here, we cloned and functionally analyzed the macaque and marmoset orthologues of human TMPRSS2. In addition, we analyzed the macaque orthologues of human TMPRSS4 and HAT, which also belong to the TTSP family. We found that all NHP orthologues of human TMPRSS2, TMPRSS4 and HAT cleave and activate HA upon directed expression and provide evidence that endogenous TMPRSS2 is expressed in the respiratory epithelium of rhesus macaques. Finally, we demonstrate that a serine protease inhibitor active against TMPRSS2 suppresses FLUAV spread in precision-cut lung slices of human, macaque and marmoset origin. These results indicate that FLUAV depends on serine protease activity for spread in diverse NHP and in humans. Moreover, our findings suggest that macaques and marmosets may serve as models to study FLUAV activation by TMPRSS2 in human patients."],["dc.identifier.doi","10.1371/journal.pone.0176597"],["dc.identifier.pmid","28493964"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14490"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58876"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Non-human primate orthologues of TMPRSS2 cleave and activate the influenza virus hemagglutinin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]