Pöhlmann, Stefan

[["dc.bibliographiccitation.firstpage","2034"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Emerging Infectious Diseases"],["dc.bibliographiccitation.lastpage","2036"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Gierer, Stefanie"],["dc.contributor.author","Hofmann-Winkler, Heike"],["dc.contributor.author","Albuali, Waleed H."],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Al-Rubaish, Abdullah M."],["dc.contributor.author","Yousef, Abdullah A."],["dc.contributor.author","Al-Nafaie, Awatif N."],["dc.contributor.author","Al-Ali, Amein K."],["dc.contributor.author","Obeid, Obeid E."],["dc.contributor.author","Alkharsah, Khaled R."],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2022-10-06T13:26:39Z"],["dc.date.available","2022-10-06T13:26:39Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.3201/eid1912.130701"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115131"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1080-6059"],["dc.relation.issn","1080-6040"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Lack of MERS Coronavirus Neutralizing Antibodies in Humans, Eastern Province, Saudi Arabia"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6150"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.lastpage","6160"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Dijkman, Ronald"],["dc.contributor.author","Habjan, Matthias"],["dc.contributor.author","Heurich, Adeline"],["dc.contributor.author","Gierer, Stefanie"],["dc.contributor.author","Glowacka, Ilona"],["dc.contributor.author","Welsch, Kathrin"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Schneider, Heike"],["dc.contributor.author","Hofmann-Winkler, Heike"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2022-10-06T13:25:38Z"],["dc.date.available","2022-10-06T13:25:38Z"],["dc.date.issued","2013"],["dc.description.abstract","ABSTRACT\n \n Infection with human coronavirus 229E (HCoV-229E) is associated with the common cold and may result in pneumonia in immunocompromised patients. The viral spike (S) protein is incorporated into the viral envelope and mediates infectious entry of HCoV-229E into host cells, a process that depends on the activation of the S-protein by host cell proteases. However, the proteases responsible for HCoV-229E activation are incompletely defined. Here we show that the type II transmembrane serine proteases TMPRSS2 and HAT cleave the HCoV-229E S-protein (229E-S) and augment 229E-S-driven cell-cell fusion, suggesting that TMPRSS2 and HAT can activate 229E-S. Indeed, engineered expression of TMPRSS2 and HAT rendered 229E-S-driven virus-cell fusion insensitive to an inhibitor of cathepsin L, a protease previously shown to facilitate HCoV-229E infection. Inhibition of endogenous cathepsin L or TMPRSS2 demonstrated that both proteases can activate 229E-S for entry into cells that are naturally susceptible to infection. In addition, evidence was obtained that activation by TMPRSS2 rescues 229E-S-dependent cell entry from inhibition by IFITM proteins. Finally, immunohistochemistry revealed that TMPRSS2 is coexpressed with CD13, the HCoV-229E receptor, in human airway epithelial (HAE) cells, and that CD13\n +\n TMPRSS2\n +\n cells are preferentially targeted by HCoV-229E, suggesting that TMPRSS2 can activate HCoV-229E in infected humans. In sum, our results indicate that HCoV-229E can employ redundant proteolytic pathways to ensure its activation in host cells. In addition, our observations and previous work suggest that diverse human respiratory viruses are activated by TMPRSS2, which may constitute a target for antiviral intervention."],["dc.identifier.doi","10.1128/JVI.03372-12"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114884"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1098-5514"],["dc.relation.issn","0022-538X"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights.uri","https://journals.asm.org/non-commercial-tdm-license"],["dc.title","TMPRSS2 Activates the Human Coronavirus 229E for Cathepsin-Independent Host Cell Entry and Is Expressed in Viral Target Cells in the Respiratory Epithelium"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","265"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Virology"],["dc.bibliographiccitation.lastpage","274"],["dc.bibliographiccitation.volume","413"],["dc.contributor.author","Simmons, Graham"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Glowacka, Ilona"],["dc.contributor.author","Steffen, Imke"],["dc.contributor.author","Chaipan, Chawaree"],["dc.contributor.author","Agudelo, Juliet"],["dc.contributor.author","Lu, Kai"],["dc.contributor.author","Rennekamp, Andrew J."],["dc.contributor.author","Hofmann, Heike"],["dc.contributor.author","Bates, Paul"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2022-10-06T13:33:27Z"],["dc.date.available","2022-10-06T13:33:27Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1016/j.virol.2011.02.020"],["dc.identifier.pii","S0042682211000924"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115636"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.issn","0042-6822"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Different host cell proteases activate the SARS-coronavirus spike-protein for cell–cell and virus–cell fusion"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5502"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.lastpage","5511"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Gierer, Stefanie"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Kaup, Franziska"],["dc.contributor.author","Wrensch, Florian"],["dc.contributor.author","Heurich, Adeline"],["dc.contributor.author","Krämer-Kühl, Annika"],["dc.contributor.author","Welsch, Kathrin"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Meyer, Benjamin"],["dc.contributor.author","Drosten, Christian"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2022-10-06T13:25:31Z"],["dc.date.available","2022-10-06T13:25:31Z"],["dc.date.issued","2013"],["dc.description.abstract","ABSTRACT\n The novel human coronavirus EMC (hCoV-EMC), which recently emerged in Saudi Arabia, is highly pathogenic and could pose a significant threat to public health. The elucidation of hCoV-EMC interactions with host cells is critical to our understanding of the pathogenesis of this virus and to the identification of targets for antiviral intervention. Here we investigated the viral and cellular determinants governing hCoV-EMC entry into host cells. We found that the spike protein of hCoV-EMC (EMC-S) is incorporated into lentiviral particles and mediates transduction of human cell lines derived from different organs, including the lungs, kidneys, and colon, as well as primary human macrophages. Expression of the known coronavirus receptors ACE2, CD13, and CEACAM1 did not facilitate EMC-S-driven transduction, suggesting that hCoV-EMC uses a novel receptor for entry. Directed protease expression and inhibition analyses revealed that TMPRSS2 and endosomal cathepsins activate EMC-S for virus-cell fusion and constitute potential targets for antiviral intervention. Finally, EMC-S-driven transduction was abrogated by serum from an hCoV-EMC-infected patient, indicating that EMC-S-specific neutralizing antibodies can be generated in patients. Collectively, our results indicate that hCoV-EMC uses a novel receptor for protease-activated entry into human cells and might be capable of extrapulmonary spread. In addition, they define TMPRSS2 and cathepsins B and L as potential targets for intervention and suggest that neutralizing antibodies contribute to the control of hCoV-EMC infection."],["dc.identifier.doi","10.1128/JVI.00128-13"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114860"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1098-5514"],["dc.relation.issn","0022-538X"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights.uri","https://journals.asm.org/non-commercial-tdm-license"],["dc.title","The Spike Protein of the Emerging Betacoronavirus EMC Uses a Novel Coronavirus Receptor for Entry, Can Be Activated by TMPRSS2, and Is Targeted by Neutralizing Antibodies"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e43337"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Gnirß, Kerstin"],["dc.contributor.author","Nehlmeier, Inga"],["dc.contributor.author","Gawanbacht, Ali"],["dc.contributor.author","Kirchhoff, Frank"],["dc.contributor.author","Ehrhardt, Christina"],["dc.contributor.author","Ludwig, Stephan"],["dc.contributor.author","Kiene, Miriam"],["dc.contributor.author","Moldenhauer, Anna-Sophie"],["dc.contributor.author","Goedecke, Ulrike"],["dc.contributor.author","Karsten, Christina B."],["dc.contributor.author","Kühl, Annika"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2019-07-09T11:53:44Z"],["dc.date.available","2019-07-09T11:53:44Z"],["dc.date.issued","2012"],["dc.description.abstract","The interferon-induced host cell factor tetherin inhibits release of human immunodeficiency virus (HIV) from the plasma membrane of infected cells and is counteracted by the HIV-1 protein Vpu. Influenza A virus (FLUAV) also buds from the plasma membrane and is not inhibited by tetherin. Here, we investigated if FLUAV encodes a functional equivalent of Vpu for tetherin antagonism. We found that expression of the FLUAV protein NS1, which antagonizes the interferon (IFN) response, did not block the tetherin-mediated restriction of HIV release, which was rescued by Vpu. Similarly, tetherinmediated inhibition of HIV release was not rescued by FLUAV infection. In contrast, FLUAV infection induced tetherin expression on target cells in an IFN-dependent manner. These results suggest that FLUAV escapes the antiviral effects of tetherin without encoding a tetherin antagonist with Vpu-like activity."],["dc.identifier.doi","10.1371/journal.pone.0043337"],["dc.identifier.fs","588509"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7923"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60484"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Influenza A Virus Does Not Encode a Tetherin Antagonist with Vpu-Like Activity and Induces IFN-Dependent Tetherin Expression in Infected Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Virology"],["dc.bibliographiccitation.lastpage","10"],["dc.bibliographiccitation.volume","424"],["dc.contributor.author","Gnirß, Kerstin"],["dc.contributor.author","Kühl, Annika"],["dc.contributor.author","Karsten, Christina"],["dc.contributor.author","Glowacka, Ilona"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Kaup, Franziska"],["dc.contributor.author","Hofmann, Heike"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2022-10-06T13:33:28Z"],["dc.date.available","2022-10-06T13:33:28Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1016/j.virol.2011.11.031"],["dc.identifier.pii","S004268221100568X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115637"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.issn","0042-6822"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Cathepsins B and L activate Ebola but not Marburg virus glycoproteins for efficient entry into cell lines and macrophages independent of TMPRSS2 expression"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","S850"],["dc.bibliographiccitation.issue","Suppl. 3"],["dc.bibliographiccitation.journal","The Journal of Infectious Diseases"],["dc.bibliographiccitation.lastpage","S860"],["dc.bibliographiccitation.volume","204"],["dc.contributor.author","Kühl, Annika"],["dc.contributor.author","Banning, Carina"],["dc.contributor.author","Marzi, Andrea"],["dc.contributor.author","Votteler, Jörg"],["dc.contributor.author","Steffen, Imke"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Glowacka, Ilona"],["dc.contributor.author","Konrad, Andreas"],["dc.contributor.author","Stürzl, Michael"],["dc.contributor.author","Guo, Ju-Tao"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2022-10-06T13:34:58Z"],["dc.date.available","2022-10-06T13:34:58Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1093/infdis/jir378"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/116023"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1537-6613"],["dc.relation.issn","0022-1899"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","The Ebola Virus Glycoprotein and HIV-1 Vpu Employ Different Strategies to Counteract the Antiviral Factor Tetherin"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4122"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.lastpage","4134"],["dc.bibliographiccitation.volume","85"],["dc.contributor.author","Glowacka, Ilona"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Müller, Marcel A."],["dc.contributor.author","Allen, Paul"],["dc.contributor.author","Soilleux, Elizabeth"],["dc.contributor.author","Pfefferle, Susanne"],["dc.contributor.author","Steffen, Imke"],["dc.contributor.author","Tsegaye, Theodros Solomon"],["dc.contributor.author","He, Yuxian"],["dc.contributor.author","Gnirss, Kerstin"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2022-10-06T13:25:37Z"],["dc.date.available","2022-10-06T13:25:37Z"],["dc.date.issued","2011"],["dc.description.abstract","ABSTRACT\n \n The spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) can be proteolytically activated by cathepsins B and L upon viral uptake into target cell endosomes. In contrast, it is largely unknown whether host cell proteases located in the secretory pathway of infected cells and/or on the surface of target cells can cleave SARS S. We along with others could previously show that the type II transmembrane protease TMPRSS2 activates the influenza virus hemagglutinin and the human metapneumovirus F protein by cleavage. Here, we assessed whether SARS S is proteolytically processed by TMPRSS2. Western blot analysis revealed that SARS S was cleaved into several fragments upon coexpression of TMPRSS2 (\n cis\n -cleavage) and upon contact between SARS S-expressing cells and TMPRSS2-positive cells (\n trans\n -cleavage).\n cis\n -cleavage resulted in release of SARS S fragments into the cellular supernatant and in inhibition of antibody-mediated neutralization, most likely because SARS S fragments function as antibody decoys.\n trans\n -cleavage activated SARS S on effector cells for fusion with target cells and allowed efficient SARS S-driven viral entry into targets treated with a lysosomotropic agent or a cathepsin inhibitor. Finally, ACE2, the cellular receptor for SARS-CoV, and TMPRSS2 were found to be coexpressed by type II pneumocytes, which represent important viral target cells, suggesting that SARS S is cleaved by TMPRSS2 in the lung of SARS-CoV-infected individuals. In summary, we show that TMPRSS2 might promote viral spread and pathogenesis by diminishing viral recognition by neutralizing antibodies and by activating SARS S for cell-cell and virus-cell fusion."],["dc.identifier.doi","10.1128/JVI.02232-10"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114880"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1098-5514"],["dc.relation.issn","0022-538X"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights.uri","https://journals.asm.org/non-commercial-tdm-license"],["dc.title","Evidence that TMPRSS2 Activates the Severe Acute Respiratory Syndrome Coronavirus Spike Protein for Membrane Fusion and Reduces Viral Control by the Humoral Immune Response"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","12087"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.lastpage","12097"],["dc.bibliographiccitation.volume","88"],["dc.contributor.author","Zmora, Pawel"],["dc.contributor.author","Blazejewska, Paulina"],["dc.contributor.author","Moldenhauer, Anna-Sophie"],["dc.contributor.author","Welsch, Kathrin"],["dc.contributor.author","Nehlmeier, Inga"],["dc.contributor.author","Wu, Qingyu"],["dc.contributor.author","Schneider, Heike"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.editor","Lyles, Douglas S."],["dc.date.accessioned","2022-10-06T13:25:35Z"],["dc.date.available","2022-10-06T13:25:35Z"],["dc.date.issued","2014"],["dc.description.abstract","ABSTRACT\n The type II transmembrane serine protease (TTSP) TMPRSS2 cleaves and activates the influenza virus and coronavirus surface proteins. Expression of TMPRSS2 is essential for the spread and pathogenesis of H1N1 influenza viruses in mice. In contrast, H3N2 viruses are less dependent on TMPRSS2 for viral amplification, suggesting that these viruses might employ other TTSPs for their activation. Here, we analyzed TTSPs, reported to be expressed in the respiratory system, for the ability to activate influenza viruses and coronaviruses. We found that MSPL and, to a lesser degree, DESC1 are expressed in human lung tissue and cleave and activate the spike proteins of the Middle East respiratory syndrome and severe acute respiratory syndrome coronaviruses for cell-cell and virus-cell fusion. In addition, we show that these proteases support the spread of all influenza virus subtypes previously pandemic in humans. In sum, we identified two host cell proteases that could promote the amplification of influenza viruses and emerging coronaviruses in humans and might constitute targets for antiviral intervention.\n \n IMPORTANCE\n Activation of influenza viruses by host cell proteases is essential for viral infectivity and the enzymes responsible are potential targets for antiviral intervention. The present study demonstrates that two cellular serine proteases, DESC1 and MSPL, activate influenza viruses and emerging coronaviruses in cell culture and, because of their expression in human lung tissue, might promote viral spread in the infected host. Antiviral strategies aiming to prevent viral activation might thus need to encompass inhibitors targeting MSPL and DESC1."],["dc.identifier.doi","10.1128/JVI.01427-14"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114873"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1098-5514"],["dc.relation.issn","0022-538X"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights.uri","https://journals.asm.org/non-commercial-tdm-license"],["dc.title","DESC1 and MSPL Activate Influenza A Viruses and Emerging Coronaviruses for Host Cell Entry"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e35876"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Heurich, Adeline"],["dc.contributor.author","Lavender, Hayley"],["dc.contributor.author","Gierer, Stefanie"],["dc.contributor.author","Danisch, Simon"],["dc.contributor.author","Perin, Paula"],["dc.contributor.author","Lucas, Jared M."],["dc.contributor.author","Nelson, Peter S."],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Soilleux, Elizabeth J."],["dc.date.accessioned","2019-07-09T11:53:44Z"],["dc.date.available","2019-07-09T11:53:44Z"],["dc.date.issued","2012"],["dc.description.abstract","The type II transmembrane serine proteases TMPRSS2 and HAT activate influenza viruses and the SARS-coronavirus (TMPRSS2) in cell culture and may play an important role in viral spread and pathogenesis in the infected host. However, it is at present largely unclear to what extent these proteases are expressed in viral target cells in human tissues. Here, we show that both HAT and TMPRSS2 are coexpressed with 2,6-linked sialic acids, the major receptor determinant of human influenza viruses, throughout the human respiratory tract. Similarly, coexpression of ACE2, the SARS-coronavirus receptor, and TMPRSS2 was frequently found in the upper and lower aerodigestive tract, with the exception of the vocal folds, epiglottis and trachea. Finally, activation of influenza virus was conserved between human, avian and porcine TMPRSS2, suggesting that this protease might activate influenza virus in reservoir-, intermediate- and human hosts. In sum, our results show that TMPRSS2 and HAT are expressed by important influenza and SARS-coronavirus target cells and could thus support viral spread in the human host."],["dc.identifier.doi","10.1371/journal.pone.0035876"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7927"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60485"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Influenza and SARS-Coronavirus Activating Proteases TMPRSS2 and HAT Are Expressed at Multiple Sites in Human Respiratory and Gastrointestinal Tracts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]