Pöhlmann, Stefan

[["dc.bibliographiccitation.artnumber","e0152134"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PloS one"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Krüger, Nadine"],["dc.contributor.author","Zmora, Pawel"],["dc.contributor.author","Wrensch, Florian"],["dc.contributor.author","Herrler, Georg"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2019-07-09T11:42:14Z"],["dc.date.available","2019-07-09T11:42:14Z"],["dc.date.issued","2016"],["dc.description.abstract","New World bats have recently been discovered to harbor influenza A virus (FLUAV)-related viruses, termed bat-associated influenza A-like viruses (batFLUAV). The internal proteins of batFLUAV are functional in mammalian cells. In contrast, no biological functionality could be demonstrated for the surface proteins, hemagglutinin (HA)-like (HAL) and neuraminidase (NA)-like (NAL), and these proteins need to be replaced by their human counterparts to allow spread of batFLUAV in human cells. Here, we employed rhabdoviral vectors to study the role of HAL and NAL in viral entry. Vectors pseudotyped with batFLUAV-HAL and -NAL were able to enter bat cells but not cells from other mammalian species. Host cell entry was mediated by HAL and was dependent on prior proteolytic activation of HAL and endosomal low pH. In contrast, sialic acids were dispensable for HAL-driven entry. Finally, the type II transmembrane serine protease TMPRSS2 was able to activate HAL for cell entry indicating that batFLUAV can utilize human proteases for HAL activation. Collectively, these results identify viral and cellular factors governing host cell entry driven by batFLUAV surface proteins. They suggest that the absence of a functional receptor precludes entry of batFLUAV into human cells while other prerequisites for entry, HAL activation and protonation, are met in target cells of human origin."],["dc.identifier.doi","10.1371/journal.pone.0152134"],["dc.identifier.pmid","27028521"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13149"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58625"],["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","The Hemagglutinin of Bat-Associated Influenza Viruses Is Activated by TMPRSS2 for pH-Dependent Entry into Bat but Not Human Cells."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Viruses"],["dc.bibliographiccitation.volume","14"],["dc.contributor.affiliation","Jäger, Niklas; 1Infection Biology Unit, German Primate Center–Leibniz Institute for Primate Research, 37077 Göttingen, Germany; njaeger@dpz.eu (N.J.); mhoffmann@dpz.eu (M.H.); spoehlmann@dpz.eu (S.P.)"],["dc.contributor.affiliation","Hoffmann, Markus; 1Infection Biology Unit, German Primate Center–Leibniz Institute for Primate Research, 37077 Göttingen, Germany; njaeger@dpz.eu (N.J.); mhoffmann@dpz.eu (M.H.); spoehlmann@dpz.eu (S.P.)"],["dc.contributor.affiliation","Pöhlmann, Stefan; 1Infection Biology Unit, German Primate Center–Leibniz Institute for Primate Research, 37077 Göttingen, Germany; njaeger@dpz.eu (N.J.); mhoffmann@dpz.eu (M.H.); spoehlmann@dpz.eu (S.P.)"],["dc.contributor.affiliation","Krüger, Nadine; 1Infection Biology Unit, German Primate Center–Leibniz Institute for Primate Research, 37077 Göttingen, Germany; njaeger@dpz.eu (N.J.); mhoffmann@dpz.eu (M.H.); spoehlmann@dpz.eu (S.P.)"],["dc.contributor.author","Jäger, Niklas"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Krüger, Nadine"],["dc.date.accessioned","2022-08-04T08:22:41Z"],["dc.date.available","2022-08-04T08:22:41Z"],["dc.date.issued","2022-07-13"],["dc.date.updated","2022-08-03T16:09:28Z"],["dc.description.sponsorship","DFG Priority program “Innate Sensing and Restriction of Retroviruses”"],["dc.description.sponsorship","Federal Ministry of Education and Research"],["dc.description.sponsorship","Ministry of Lower Saxony"],["dc.identifier.doi","10.3390/v14071526"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112621"],["dc.language.iso","en"],["dc.relation.eissn","1999-4915"],["dc.rights","CC BY 4.0"],["dc.title","Nafamostat-Mediated Inhibition of SARS-CoV-2 Ribosomal Frameshifting Is Insufficient to Impair Viral Replication in Vero Cells. Comment on Munshi et al. Identifying Inhibitors of −1 Programmed Ribosomal Frameshifting in a Broad Spectrum of Coronaviruses. Viruses 2022, 14, 177"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0214968"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Plegge, Teresa"],["dc.contributor.author","Spiegel, Martin"],["dc.contributor.author","Krüger, Nadine"],["dc.contributor.author","Nehlmeier, Inga"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","González Hernández, Mariana"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2019-07-09T11:51:10Z"],["dc.date.available","2019-07-09T11:51:10Z"],["dc.date.issued","2019"],["dc.description.abstract","Emerging viruses such as severe fever and thrombocytopenia syndrome virus (SFTSV) and Ebola virus (EBOV) are responsible for significant morbidity and mortality. Host cell proteases that process the glycoproteins of these viruses are potential targets for antiviral intervention. The aspartyl protease signal peptide peptidase (SPP) has recently been shown to be required for processing of the glycoprotein precursor, Gn/Gc, of Bunyamwera virus and for viral infectivity. Here, we investigated whether SPP is also required for infectivity of particles bearing SFTSV-Gn/Gc. Entry driven by the EBOV glycoprotein (GP) and the Lassa virus glycoprotein (LASV-GPC) depends on the cysteine proteases cathepsin B and L (CatB/CatL) and the serine protease subtilisin/kexin-isozyme 1 (SKI-1), respectively, and was examined in parallel for control purposes. We found that inhibition of SPP and SKI-1 did not interfere with SFTSV Gn + Gc-driven entry but, unexpectedly, blocked entry mediated by EBOV-GP. The inhibition occurred at the stage of proteolytic activation and the SPP inhibitor was found to block CatL/CatB activity. In contrast, the SKI-1 inhibitor did not interfere with CatB/CatL activity but disrupted CatB localization in endo/lysosomes, the site of EBOV-GP processing. These results underline the potential of protease inhibitors for antiviral therapy but also show that previously characterized compounds might exert broader specificity than initially appreciated and might block viral entry via diverse mechanisms."],["dc.identifier.doi","10.1371/journal.pone.0214968"],["dc.identifier.pmid","30973897"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16063"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59889"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","599"],["dc.title","Inhibitors of signal peptide peptidase and subtilisin/kexin-isozyme 1 inhibit Ebola virus glycoprotein-driven cell entry by interfering with activity and cellular localization of endosomal cathepsins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","828"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Viruses"],["dc.bibliographiccitation.volume","14"],["dc.contributor.affiliation","Färber, Iris; 1Department of Pathology, University of Veterinary Medicine, Foundation, 30559 Hannover, Germany; iris.verena.faerber@tiho-hannover.de (I.F.); johannes.krueger@tiho-hannover.de (J.K.); federico.armando@tiho-hannover.de (F.A.); sandra.runft@tiho-hannover.de (S.R.)"],["dc.contributor.affiliation","Krüger, Johannes; 1Department of Pathology, University of Veterinary Medicine, Foundation, 30559 Hannover, Germany; iris.verena.faerber@tiho-hannover.de (I.F.); johannes.krueger@tiho-hannover.de (J.K.); federico.armando@tiho-hannover.de (F.A.); sandra.runft@tiho-hannover.de (S.R.)"],["dc.contributor.affiliation","Rocha, Cheila; 2Infection Biology Unit, German Primate Center, Leibniz Institute for Primate Research, 37077 Göttingen, Germany; crocha@dpz.eu (C.R.); spoehlmann@dpz.eu (S.P.); nkrueger@dpz.eu (N.K.)"],["dc.contributor.affiliation","Armando, Federico; 1Department of Pathology, University of Veterinary Medicine, Foundation, 30559 Hannover, Germany; iris.verena.faerber@tiho-hannover.de (I.F.); johannes.krueger@tiho-hannover.de (J.K.); federico.armando@tiho-hannover.de (F.A.); sandra.runft@tiho-hannover.de (S.R.)"],["dc.contributor.affiliation","von Köckritz-Blickwede, Maren; 3Department of Biochemistry, University of Veterinary Medicine Hannover, Foundation, 30559 Hannover, Germany; maren.von.koeckritz-blickwede@tiho-hannover.de"],["dc.contributor.affiliation","Pöhlmann, Stefan; 2Infection Biology Unit, German Primate Center, Leibniz Institute for Primate Research, 37077 Göttingen, Germany; crocha@dpz.eu (C.R.); spoehlmann@dpz.eu (S.P.); nkrueger@dpz.eu (N.K.)"],["dc.contributor.affiliation","Braun, Armin; 6Fraunhofer Institute for Toxicology and Experimental Medicine ITEM, 30625 Hannover, Germany; braun.armin@mh-hannover.de"],["dc.contributor.affiliation","Baumgärtner, Wolfgang; 1Department of Pathology, University of Veterinary Medicine, Foundation, 30559 Hannover, Germany; iris.verena.faerber@tiho-hannover.de (I.F.); johannes.krueger@tiho-hannover.de (J.K.); federico.armando@tiho-hannover.de (F.A.); sandra.runft@tiho-hannover.de (S.R.)"],["dc.contributor.affiliation","Runft, Sandra; 1Department of Pathology, University of Veterinary Medicine, Foundation, 30559 Hannover, Germany; iris.verena.faerber@tiho-hannover.de (I.F.); johannes.krueger@tiho-hannover.de (J.K.); federico.armando@tiho-hannover.de (F.A.); sandra.runft@tiho-hannover.de (S.R.)"],["dc.contributor.affiliation","Krüger, Nadine; 2Infection Biology Unit, German Primate Center, Leibniz Institute for Primate Research, 37077 Göttingen, Germany; crocha@dpz.eu (C.R.); spoehlmann@dpz.eu (S.P.); nkrueger@dpz.eu (N.K.)"],["dc.contributor.author","Färber, Iris"],["dc.contributor.author","Krüger, Johannes"],["dc.contributor.author","Rocha, Cheila"],["dc.contributor.author","Armando, Federico"],["dc.contributor.author","von Köckritz-Blickwede, Maren"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Braun, Armin"],["dc.contributor.author","Baumgärtner, Wolfgang"],["dc.contributor.author","Runft, Sandra"],["dc.contributor.author","Krüger, Nadine"],["dc.date.accessioned","2022-05-02T08:09:39Z"],["dc.date.available","2022-05-02T08:09:39Z"],["dc.date.issued","2022"],["dc.date.updated","2022-05-05T16:06:54Z"],["dc.description.abstract","Several animal species are susceptible to SARS-CoV-2 infection, as documented by case reports and serological and in vivo infection studies. However, the susceptibility of many animal species remains unknown. Furthermore, the expression patterns of SARS-CoV-2 entry factors, such as the receptor angiotensin-converting enzyme 2 (ACE2), as well as transmembrane protease serine subtype 2 (TMPRSS2) and cathepsin L (CTSL), cellular proteases involved in SARS-CoV-2 spike protein activation, are largely unexplored in most species. Here, we generated primary cell cultures from the respiratory tract of domestic and wildlife animals to assess their susceptibility to SARS-CoV-2 infection. Additionally, the presence of ACE2, TMPRSS2 and CTSL within respiratory tract compartments was investigated in a range of animals, some with unknown susceptibility to SARS-CoV-2. Productive viral replication was observed in the nasal mucosa explants and precision-cut lung slices from dogs and hamsters, whereas culture models from ferrets and multiple ungulate species were non-permissive to infection. Overall, whereas TMPRSS2 and CTSL were equally expressed in the respiratory tract, the expression levels of ACE2 were more variable, suggesting that a restricted availability of ACE2 may contribute to reduced susceptibility. Summarized, the experimental infection of primary respiratory tract cell cultures, as well as an analysis of entry-factor distribution, enable screening for SARS-CoV-2 animal reservoirs."],["dc.description.abstract","Several animal species are susceptible to SARS-CoV-2 infection, as documented by case reports and serological and in vivo infection studies. However, the susceptibility of many animal species remains unknown. Furthermore, the expression patterns of SARS-CoV-2 entry factors, such as the receptor angiotensin-converting enzyme 2 (ACE2), as well as transmembrane protease serine subtype 2 (TMPRSS2) and cathepsin L (CTSL), cellular proteases involved in SARS-CoV-2 spike protein activation, are largely unexplored in most species. Here, we generated primary cell cultures from the respiratory tract of domestic and wildlife animals to assess their susceptibility to SARS-CoV-2 infection. Additionally, the presence of ACE2, TMPRSS2 and CTSL within respiratory tract compartments was investigated in a range of animals, some with unknown susceptibility to SARS-CoV-2. Productive viral replication was observed in the nasal mucosa explants and precision-cut lung slices from dogs and hamsters, whereas culture models from ferrets and multiple ungulate species were non-permissive to infection. Overall, whereas TMPRSS2 and CTSL were equally expressed in the respiratory tract, the expression levels of ACE2 were more variable, suggesting that a restricted availability of ACE2 may contribute to reduced susceptibility. Summarized, the experimental infection of primary respiratory tract cell cultures, as well as an analysis of entry-factor distribution, enable screening for SARS-CoV-2 animal reservoirs."],["dc.identifier.doi","10.3390/v14040828"],["dc.identifier.pii","v14040828"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/107428"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-561"],["dc.relation.eissn","1999-4915"],["dc.title","Investigations on SARS-CoV-2 Susceptibility of Domestic and Wild Animals Using Primary Cell Culture Models Derived from the Upper and Lower Respiratory Tract"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","2475"],["dc.bibliographiccitation.firstpage","2475"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Viruses"],["dc.bibliographiccitation.volume","14"],["dc.contributor.affiliation","Sidarovich, Anzhalika; 1Infection Biology Unit, German Primate Center, 37077 Göttingen, Germany"],["dc.contributor.affiliation","Krüger, Nadine; 1Infection Biology Unit, German Primate Center, 37077 Göttingen, Germany"],["dc.contributor.affiliation","Rocha, Cheila; 1Infection Biology Unit, German Primate Center, 37077 Göttingen, Germany"],["dc.contributor.affiliation","Graichen, Luise; 1Infection Biology Unit, German Primate Center, 37077 Göttingen, Germany"],["dc.contributor.affiliation","Kempf, Amy; 1Infection Biology Unit, German Primate Center, 37077 Göttingen, Germany"],["dc.contributor.affiliation","Nehlmeier, Inga; 1Infection Biology Unit, German Primate Center, 37077 Göttingen, Germany"],["dc.contributor.affiliation","Lier, Martin; 3Department of Anesthesiology, University of Göttingen Medical Center, Georg-August University of Göttingen, Robert-Koch-Straße 40, 37075 Göttingen, Germany"],["dc.contributor.affiliation","Cossmann, Anne; 4Department for Rheumatology and Immunology, Hannover Medical School, 30625 Hannover, Germany"],["dc.contributor.affiliation","Stankov, Metodi V.; 4Department for Rheumatology and Immunology, Hannover Medical School, 30625 Hannover, Germany"],["dc.contributor.affiliation","Schulz, Sebastian R.; 6Division of Molecular Immunology, Department of Internal Medicine 3, Friedrich-Alexander University of Erlangen-Nürnberg, 91054 Erlangen, Germany"],["dc.contributor.affiliation","Behrens, Georg M. N.; 4Department for Rheumatology and Immunology, Hannover Medical School, 30625 Hannover, Germany"],["dc.contributor.affiliation","Jäck, Hans-Martin; 6Division of Molecular Immunology, Department of Internal Medicine 3, Friedrich-Alexander University of Erlangen-Nürnberg, 91054 Erlangen, Germany"],["dc.contributor.affiliation","Pöhlmann, Stefan; 1Infection Biology Unit, German Primate Center, 37077 Göttingen, Germany"],["dc.contributor.affiliation","Hoffmann, Markus; 1Infection Biology Unit, German Primate Center, 37077 Göttingen, Germany"],["dc.contributor.author","Sidarovich, Anzhalika"],["dc.contributor.author","Krüger, Nadine"],["dc.contributor.author","Rocha, Cheila"],["dc.contributor.author","Graichen, Luise"],["dc.contributor.author","Kempf, Amy"],["dc.contributor.author","Nehlmeier, Inga"],["dc.contributor.author","Lier, Martin"],["dc.contributor.author","Cossmann, Anne"],["dc.contributor.author","Stankov, Metodi V."],["dc.contributor.author","Schulz, Sebastian R."],["dc.contributor.author","Behrens, Georg M. N."],["dc.contributor.author","Jäck, Hans-Martin"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Hoffmann, Markus"],["dc.date.accessioned","2022-12-07T15:54:47Z"],["dc.date.available","2022-12-07T15:54:47Z"],["dc.date.issued","2022-11-09"],["dc.date.updated","2022-12-07T14:20:25Z"],["dc.description.abstract","The spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) facilitates viral entry into host cells and is the key target for neutralizing antibodies. The SARS-CoV-2 lineage B.1.620 carries fifteen mutations in the S protein and is spread in Africa, the US and Europe, while lineage R.1 harbors four mutations in S and infections were observed in several countries, particularly Japan and the US. However, the impact of the mutations in B.1.620 and R.1 S proteins on antibody-mediated neutralization and host cell entry are largely unknown. Here, we report that these mutations are compatible with robust ACE2 binding and entry into cell lines, and they markedly reduce neutralization by vaccine-induced antibodies. Our results reveal evasion of neutralizing antibodies by B.1.620 and R.1, which might have contributed to the spread of these lineages."],["dc.description.sponsorship","German Federal Ministry of Education and Research (Bundesministerium für Bildung und Forschung)"],["dc.description.sponsorship","NaFoUniMedCovid19-COVIM"],["dc.description.sponsorship","Ministry for Science and Culture of Lower Saxony (Niedersächsisches Ministerium für Wissenschaft und Kultur)"],["dc.description.sponsorship","Bavarian State Ministry for Science and the Arts"],["dc.description.sponsorship","German Research Foundation (Deutsche Forschungsgemeinschaft)"],["dc.description.sponsorship","German Center for Infection Research"],["dc.description.sponsorship","European Regional Development Fund"],["dc.identifier.doi","10.3390/v14112475"],["dc.identifier.pii","v14112475"],["dc.identifier.pmid","36366573"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/118483"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-621"],["dc.relation.eissn","1999-4915"],["dc.relation.issn","1999-4915"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights","CC BY 4.0"],["dc.title","Host Cell Entry and Neutralization Sensitivity of SARS-CoV-2 Lineages B.1.620 and R.1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]