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.artnumber","S2211124721008287"],["dc.bibliographiccitation.firstpage","109415"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Hofmann-Winkler, Heike"],["dc.contributor.author","Krüger, Nadine"],["dc.contributor.author","Kempf, Amy"],["dc.contributor.author","Nehlmeier, Inga"],["dc.contributor.author","Graichen, Luise"],["dc.contributor.author","Arora, Prerna"],["dc.contributor.author","Sidarovich, Anzhalika"],["dc.contributor.author","Moldenhauer, Anna-Sophie"],["dc.contributor.author","Winkler, Martin S."],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2021-09-01T06:42:36Z"],["dc.date.available","2021-09-01T06:42:36Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.celrep.2021.109415"],["dc.identifier.pii","S2211124721008287"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89097"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation.issn","2211-1247"],["dc.title","SARS-CoV-2 variant B.1.617 is resistant to bamlanivimab and evades antibodies induced by infection and vaccination"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10636"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Krüger, Nadine"],["dc.contributor.author","Rocha, Cheila"],["dc.contributor.author","Runft, Sandra"],["dc.contributor.author","Krüger, Johannes"],["dc.contributor.author","Färber, Iris"],["dc.contributor.author","Armando, Federico"],["dc.contributor.author","Leitzen, Eva"],["dc.contributor.author","Brogden, Graham"],["dc.contributor.author","Gerold, Gisa"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Baumgärtner, Wolfgang"],["dc.date.accessioned","2021-12-01T09:24:06Z"],["dc.date.available","2021-12-01T09:24:06Z"],["dc.date.issued","2021"],["dc.description.abstract","Natural or experimental infection of domestic cats and virus transmission from humans to captive predatory cats suggest that felids are highly susceptible to SARS-CoV-2 infection. However, it is unclear which cells and compartments of the respiratory tract are infected. To address this question, primary cell cultures derived from the nose, trachea, and lungs of cat and lion were inoculated with SARS-CoV-2. Strong viral replication was observed for nasal mucosa explants and tracheal air–liquid interface cultures, whereas replication in lung slices was less efficient. Infection was mainly restricted to epithelial cells and did not cause major pathological changes. Detection of high ACE2 levels in the nose and trachea but not lung further suggests that susceptibility of feline tissues to SARS-CoV-2 correlates with ACE2 expression. Collectively, this study demonstrates that SARS-CoV-2 can efficiently replicate in the feline upper respiratory tract ex vivo and thus highlights the risk of SARS-CoV-2 spillover from humans to felids."],["dc.description.abstract","Natural or experimental infection of domestic cats and virus transmission from humans to captive predatory cats suggest that felids are highly susceptible to SARS-CoV-2 infection. However, it is unclear which cells and compartments of the respiratory tract are infected. To address this question, primary cell cultures derived from the nose, trachea, and lungs of cat and lion were inoculated with SARS-CoV-2. Strong viral replication was observed for nasal mucosa explants and tracheal air–liquid interface cultures, whereas replication in lung slices was less efficient. Infection was mainly restricted to epithelial cells and did not cause major pathological changes. Detection of high ACE2 levels in the nose and trachea but not lung further suggests that susceptibility of feline tissues to SARS-CoV-2 correlates with ACE2 expression. Collectively, this study demonstrates that SARS-CoV-2 can efficiently replicate in the feline upper respiratory tract ex vivo and thus highlights the risk of SARS-CoV-2 spillover from humans to felids."],["dc.identifier.doi","10.3390/ijms221910636"],["dc.identifier.pii","ijms221910636"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94846"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","1422-0067"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","The Upper Respiratory Tract of Felids Is Highly Susceptible to SARS-CoV-2 Infection"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","109017"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.volume","35"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Zhang, Lu"],["dc.contributor.author","Krüger, Nadine"],["dc.contributor.author","Graichen, Luise"],["dc.contributor.author","Kleine-Weber, Hannah"],["dc.contributor.author","Hofmann-Winkler, Heike"],["dc.contributor.author","Kempf, Amy"],["dc.contributor.author","Nessler, Stefan"],["dc.contributor.author","Riggert, Joachim"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2021-06-01T09:41:14Z"],["dc.date.available","2021-06-01T09:41:14Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.celrep.2021.109017"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84853"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.issn","2211-1247"],["dc.title","SARS-CoV-2 mutations acquired in mink reduce antibody-mediated neutralization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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.issue","3"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.volume","93"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Nehlmeier, Inga"],["dc.contributor.author","Brinkmann, Constantin"],["dc.contributor.author","Krähling, Verena"],["dc.contributor.author","Behner, Laura"],["dc.contributor.author","Moldenhauer, Anna-Sophie"],["dc.contributor.author","Krüger, Nadine"],["dc.contributor.author","Nehls, Julia"],["dc.contributor.author","Schindler, Michael"],["dc.contributor.author","Hoenen, Thomas"],["dc.contributor.author","Maisner, Andrea"],["dc.contributor.author","Becker, Stephan"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.editor","Dermody, Terence S."],["dc.date.accessioned","2020-12-10T18:37:03Z"],["dc.date.available","2020-12-10T18:37:03Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1128/JVI.01821-18"],["dc.identifier.eissn","1098-5514"],["dc.identifier.issn","0022-538X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76825"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Tetherin Inhibits Nipah Virus but Not Ebola Virus Replication in Fruit Bat Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","447"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","456.e11"],["dc.bibliographiccitation.volume","185"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Krüger, Nadine"],["dc.contributor.author","Schulz, Sebastian"],["dc.contributor.author","Cossmann, Anne"],["dc.contributor.author","Rocha, Cheila"],["dc.contributor.author","Kempf, Amy"],["dc.contributor.author","Nehlmeier, Inga"],["dc.contributor.author","Graichen, Luise"],["dc.contributor.author","Moldenhauer, Anna-Sophie"],["dc.contributor.author","Winkler, Martin S."],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2022-04-01T10:00:59Z"],["dc.date.available","2022-04-01T10:00:59Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1016/j.cell.2021.12.032"],["dc.identifier.pii","S0092867421014951"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/105571"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-530"],["dc.relation.issn","0092-8674"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","The Omicron variant is highly resistant against antibody-mediated neutralization: Implications for control of the COVID-19 pandemic"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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","103255"],["dc.bibliographiccitation.journal","EBioMedicine"],["dc.bibliographiccitation.volume","65"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Hofmann-Winkler, Heike"],["dc.contributor.author","Smith, Joan C."],["dc.contributor.author","Krüger, Nadine"],["dc.contributor.author","Arora, Prerna"],["dc.contributor.author","Sørensen, Lambert K."],["dc.contributor.author","Søgaard, Ole S."],["dc.contributor.author","Hasselstrøm, Jørgen Bo"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Hempel, Tim"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2022-10-06T13:33:05Z"],["dc.date.available","2022-10-06T13:33:05Z"],["dc.date.issued","2021"],["dc.description.sponsorship"," http://dx.doi.org/10.13039/100010663 ERC"],["dc.description.sponsorship"," http://dx.doi.org/10.13039/501100004937 Bundesministerium fur Bildung und Forschung Dienststelle Berlin"],["dc.description.sponsorship"," http://dx.doi.org/10.13039/501100001659 Deutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.1016/j.ebiom.2021.103255"],["dc.identifier.pii","S2352396421000487"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115541"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.issn","2352-3964"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Camostat mesylate inhibits SARS-CoV-2 activation by TMPRSS2-related proteases and its metabolite GBPA exerts antiviral activity"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]