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Article ; Online: pH inactivation of SARS-CoV-2 and SARS-CoV in virus spiked protein A eluates from a mAb purification process.

Limburg, Hannah / Schwerdtner, Marie / Wilson, Eileen / Roth, Bernhard / Cassart, Jean-Pol / Werner, Anke-Dorothee / Harbig, Anne / Böttcher-Friebertshäuser, Eva / Stokes, Anne

Biologicals : journal of the International Association of Biological Standardization

2024 Volume 86, Page(s) 101753

Abstract: Biopharmaceutical manufacturing processes may include a low pH treatment step as a means of inactivating enveloped viruses. Small scale virus clearance studies are routinely performed using model enveloped viruses such as murine leukemia virus to assess ... ...

Abstract	Biopharmaceutical manufacturing processes may include a low pH treatment step as a means of inactivating enveloped viruses. Small scale virus clearance studies are routinely performed using model enveloped viruses such as murine leukemia virus to assess inactivation at the pH range used in the downstream manufacturing process. Further, as a means of bioburden reduction, chromatography resins may be cleaned and stored using sodium hydroxide and this can also inactivate viruses. The susceptibility of SARS-CoV-2 and SARS-CoV to low pH conditions using protein A eluate derived material from a monoclonal antibody production process as well as high pH cleaning conditions was addressed. SARS-CoV-2 was effectively inactivated at pH 3.0, moderately inactivated at pH 3.4, but not inactivated at pH 3.8. Low pH was less effective at inactivating SARS-CoV. Both viruses were inactivated at a high pH of ca.13.4. These studies provide important information regarding the effectiveness of viral clearance and inactivation steps of novel coronaviruses when compared to other enveloped viruses.
Language	English
Publishing date	2024-03-14
Publishing country	England
Document type	Journal Article
ZDB-ID	1017370-5
ISSN	1095-8320 ; 1045-1056
ISSN (online)	1095-8320
ISSN	1045-1056
DOI	10.1016/j.biologicals.2024.101753
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Article ; Online: ACE2 acts as a novel regulator of TMPRSS2-catalyzed proteolytic activation of influenza A virus in airway cells.

Heindl, Miriam Ruth / Rupp, Anna-Lena / Schwerdtner, Marie / Bestle, Dorothea / Harbig, Anne / De Rocher, Amy / Schmacke, Luna C / Staker, Bart / Steinmetzer, Torsten / Stein, David A / Moulton, Hong M / Böttcher-Friebertshäuser, Eva

Journal of virology

2024 Volume 98, Issue 4, Page(s) e0010224

Abstract: The transmembrane serine protease 2 (TMPRSS2) activates the outer structural proteins of a number of respiratory viruses including influenza A virus (IAV), parainfluenza viruses, and various coronaviruses for membrane fusion. Previous studies showed that ...

Abstract	The transmembrane serine protease 2 (TMPRSS2) activates the outer structural proteins of a number of respiratory viruses including influenza A virus (IAV), parainfluenza viruses, and various coronaviruses for membrane fusion. Previous studies showed that TMPRSS2 interacts with the carboxypeptidase angiotensin-converting enzyme 2 (ACE2), a cell surface protein that serves as an entry receptor for some coronaviruses. Here, by using protease activity assays, we determine that ACE2 increases the enzymatic activity of TMPRSS2 in a non-catalytic manner. Furthermore, we demonstrate that ACE2 knockdown inhibits TMPRSS2-mediated cleavage of IAV hemagglutinin (HA) in Calu-3 human airway cells and suppresses virus titers 100- to 1.000-fold. Transient expression of ACE2 in ACE2-deficient cells increased TMPRSS2-mediated HA cleavage and IAV replication. ACE2 knockdown also reduced titers of MERS-CoV and prevented S cleavage by TMPRSS2 in Calu-3 cells. By contrast, proteolytic activation and multicycle replication of IAV with multibasic HA cleavage site typically cleaved by furin were not affected by ACE2 knockdown. Co-immunoprecipitation analysis revealed that ACE2-TMPRSS2 interaction requires the enzymatic activity of TMPRSS2 and the carboxypeptidase domain of ACE2. Together, our data identify ACE2 as a new co-factor or stabilizer of TMPRSS2 activity and as a novel host cell factor involved in proteolytic activation and spread of IAV in human airway cells. Furthermore, our data indicate that ACE2 is involved in the TMPRSS2-catalyzed activation of additional respiratory viruses including MERS-CoV.IMPORTANCEProteolytic cleavage of viral envelope proteins by host cell proteases is essential for the infectivity of many viruses and relevant proteases provide promising drug targets. The transmembrane serine protease 2 (TMPRSS2) has been identified as a major activating protease of several respiratory viruses, including influenza A virus. TMPRSS2 was previously shown to interact with angiotensin-converting enzyme 2 (ACE2). Here, we report the mechanistic details of this interaction. We demonstrate that ACE2 increases or stabilizes the enzymatic activity of TMPRSS2. Furthermore, we describe ACE2 involvement in TMPRSS2-catalyzed cleavage of the influenza A virus hemagglutinin and MERS-CoV spike protein in human airway cells. These findings expand our knowledge of the activation of respiratory viruses by TMPRSS2 and the host cell factors involved. In addition, our results could help to elucidate a physiological role for TMPRSS2.
MeSH term(s)	Animals ; Dogs ; Humans ; Angiotensin-Converting Enzyme 2/deficiency ; Angiotensin-Converting Enzyme 2/genetics ; Angiotensin-Converting Enzyme 2/metabolism ; Biocatalysis ; Cell Line ; Furin/metabolism ; Hemagglutinin Glycoproteins, Influenza Virus/metabolism ; Influenza A virus/growth & development ; Influenza A virus/metabolism ; Lung/cytology ; Lung/virology ; Middle East Respiratory Syndrome Coronavirus/metabolism ; Protein Binding ; Proteolysis ; Serine Endopeptidases/metabolism ; Spike Glycoprotein, Coronavirus/metabolism ; Virus Internalization ; Virus Replication
Chemical Substances	ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; Furin (EC 3.4.21.75) ; Hemagglutinin Glycoproteins, Influenza Virus ; Serine Endopeptidases (EC 3.4.21.-) ; Spike Glycoprotein, Coronavirus ; TMPRSS2 protein, human (EC 3.4.21.-)
Language	English
Publishing date	2024-03-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.00102-24
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Article ; Online: Improving the selectivity of 3-amidinophenylalanine-derived matriptase inhibitors.

Pilgram, Oliver / Keils, Aline / Benary, Gerrit E / Müller, Janis / Merkl, Stefan / Ngaha, Sandrine / Huber, Simon / Chevillard, Florent / Harbig, Anne / Magdolen, Viktor / Heine, Andreas / Böttcher-Friebertshäuser, Eva / Steinmetzer, Torsten

European journal of medicinal chemistry

2022 Volume 238, Page(s) 114437

Abstract: A rational structure-based approach was employed to develop novel 3-amidinophenylalanine-derived matriptase inhibitors with improved selectivity against thrombin and factor Xa. Of all 23 new derivatives, several monobasic inhibitors exhibit high ... ...

Abstract	A rational structure-based approach was employed to develop novel 3-amidinophenylalanine-derived matriptase inhibitors with improved selectivity against thrombin and factor Xa. Of all 23 new derivatives, several monobasic inhibitors exhibit high matriptase affinities and strong selectivity against thrombin. Some inhibitors also possess selectivity against factor Xa, although less pronounced as found for thrombin. A crystal structure of a selective monobasic matriptase inhibitor in complex with matriptase and three crystal structures of related compounds in trypsin and thrombin have been determined. The structures offer an explanation for the different selectivity profiles of these inhibitors and contribute to a more detailed understanding of the observed structure-activity relationship. Selected compounds were tested in vitro against a matriptase-dependent H9N2 influenza virus strain and demonstrated a concentration-dependent inhibition of virus replication in MDCK(II) cells.
MeSH term(s)	Factor Xa/metabolism ; Factor Xa Inhibitors/pharmacology ; Influenza A Virus, H9N2 Subtype/metabolism ; Phenylalanine/chemistry ; Serine Endopeptidases ; Serine Proteinase Inhibitors/chemistry ; Serine Proteinase Inhibitors/pharmacology ; Structure-Activity Relationship ; Thrombin
Chemical Substances	Factor Xa Inhibitors ; Serine Proteinase Inhibitors ; Phenylalanine (47E5O17Y3R) ; Serine Endopeptidases (EC 3.4.21.-) ; matriptase (EC 3.4.21.-) ; Thrombin (EC 3.4.21.5) ; Factor Xa (EC 3.4.21.6)
Language	English
Publishing date	2022-05-12
Publishing country	France
Document type	Journal Article
ZDB-ID	188597-2
ISSN	1768-3254 ; 0009-4374 ; 0223-5234
ISSN (online)	1768-3254
ISSN	0009-4374 ; 0223-5234
DOI	10.1016/j.ejmech.2022.114437
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Article ; Online: Transcriptome profiling and protease inhibition experiments identify proteases that activate H3N2 influenza A and influenza B viruses in murine airways.

Harbig, Anne / Mernberger, Marco / Bittel, Linda / Pleschka, Stephan / Schughart, Klaus / Steinmetzer, Torsten / Stiewe, Thorsten / Nist, Andrea / Böttcher-Friebertshäuser, Eva

The Journal of biological chemistry

2020 Volume 295, Issue 33, Page(s) 11388–11407

Abstract: Cleavage of influenza virus hemagglutinin (HA) by host proteases is essential for virus infectivity. HA of most influenza A and B (IAV/IBV) viruses is cleaved at a monobasic motif by trypsin-like proteases. Previous studies have reported that ... ...

Abstract	Cleavage of influenza virus hemagglutinin (HA) by host proteases is essential for virus infectivity. HA of most influenza A and B (IAV/IBV) viruses is cleaved at a monobasic motif by trypsin-like proteases. Previous studies have reported that transmembrane serine protease 2 (TMPRSS2) is essential for activation of H7N9 and H1N1pdm IAV in mice but that H3N2 IAV and IBV activation is independent of TMPRSS2 and carried out by as-yet-undetermined protease(s). Here, to identify additional H3 IAV- and IBV-activating proteases, we used RNA-Seq to investigate the protease repertoire of murine lower airway tissues, primary type II alveolar epithelial cells (AECIIs), and the mouse lung cell line MLE-15. Among 13 candidates identified, TMPRSS4, TMPRSS13, hepsin, and prostasin activated H3 and IBV HA
MeSH term(s)	Animals ; Cell Line ; Dogs ; Enzyme Activation/drug effects ; Gene Expression Profiling ; HEK293 Cells ; Host-Pathogen Interactions/drug effects ; Humans ; Influenza A Virus, H3N2 Subtype/drug effects ; Influenza A Virus, H3N2 Subtype/physiology ; Influenza B virus/drug effects ; Influenza B virus/physiology ; Influenza, Human/drug therapy ; Influenza, Human/enzymology ; Influenza, Human/genetics ; Influenza, Human/virology ; Lung/enzymology ; Lung/metabolism ; Lung/virology ; Madin Darby Canine Kidney Cells ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Orthomyxoviridae Infections/drug therapy ; Orthomyxoviridae Infections/enzymology ; Orthomyxoviridae Infections/genetics ; Orthomyxoviridae Infections/virology ; Peptide Hydrolases/genetics ; Peptide Hydrolases/metabolism ; Protease Inhibitors/pharmacology ; Serine Endopeptidases/genetics ; Serine Endopeptidases/metabolism ; Virus Activation/drug effects
Chemical Substances	Membrane Proteins ; Protease Inhibitors ; Peptide Hydrolases (EC 3.4.-) ; Serine Endopeptidases (EC 3.4.21.-) ; Tmprss4 protein, mouse (EC 3.4.21.-)
Language	English
Publishing date	2020-04-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA120.012635
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Article ; Online: Hemagglutinins of Avian Influenza Viruses Are Proteolytically Activated by TMPRSS2 in Human and Murine Airway Cells.

Bestle, Dorothea / Limburg, Hannah / Kruhl, Diana / Harbig, Anne / Stein, David A / Moulton, Hong / Matrosovich, Mikhail / Abdelwhab, Elsayed M / Stech, Jürgen / Böttcher-Friebertshäuser, Eva

Journal of virology

2021 Volume 95, Issue 20, Page(s) e0090621

Abstract: Cleavage of the influenza A virus (IAV) hemagglutinin (HA) by host proteases is indispensable for virus replication. Most IAVs possess a monobasic HA cleavage site cleaved by trypsin-like proteases. Previously, the transmembrane protease TMPRSS2 was ... ...

Abstract	Cleavage of the influenza A virus (IAV) hemagglutinin (HA) by host proteases is indispensable for virus replication. Most IAVs possess a monobasic HA cleavage site cleaved by trypsin-like proteases. Previously, the transmembrane protease TMPRSS2 was shown to be essential for proteolytic activation of IAV HA subtypes H1, H2, H7, and H10 in mice. In contrast, additional proteases are involved in activation of certain H3 IAVs, indicating that HAs with monobasic cleavage sites can differ in their sensitivity to host proteases. Here, we investigated the role of TMPRSS2 in proteolytic activation of avian HA subtypes H1 to H11 and H14 to H16 in human and mouse airway cell cultures. Using reassortant viruses carrying representative HAs, we analyzed HA cleavage and multicycle replication in (i) lung cells of TMPRSS2-deficient mice and (ii) Calu-3 cells and primary human bronchial cells subjected to morpholino oligomer-mediated knockdown of TMPRSS2 activity. TMPRSS2 was found to be crucial for activation of H1 to H11, H14, and H15 in airway cells of human and mouse. Only H9 with an R-S-S-R cleavage site and H16 were proteolytically activated in the absence of TMPRSS2 activity, albeit with reduced efficiency. Moreover, a TMPRSS2-orthologous protease from duck supported activation of H1 to H11, H15, and H16 in MDCK cells. Together, our data demonstrate that in human and murine respiratory cells, TMPRSS2 is the major activating protease of almost all IAV HA subtypes with monobasic cleavage sites. Furthermore, our results suggest that TMPRSS2 supports activation of IAV with a monobasic cleavage site in ducks.
MeSH term(s)	Animals ; Bronchi/cytology ; Cell Line ; Dogs ; Female ; HEK293 Cells ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Hemagglutinin Glycoproteins, Influenza Virus/metabolism ; Hemagglutinins, Viral/genetics ; Hemagglutinins, Viral/metabolism ; Host-Pathogen Interactions ; Humans ; Influenza A Virus, H1N1 Subtype/physiology ; Influenza A Virus, H3N2 Subtype/physiology ; Influenza A virus/immunology ; Influenza A virus/metabolism ; Influenza A virus/pathogenicity ; Lung/virology ; Madin Darby Canine Kidney Cells ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Peptide Hydrolases/metabolism ; Proteolysis ; Respiratory Mucosa/metabolism ; Serine Endopeptidases/metabolism ; Serine Endopeptidases/physiology ; Virus Replication
Chemical Substances	Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins, Viral ; hemagglutinin, human influenza A virus ; trypsin-like serine protease ; Peptide Hydrolases (EC 3.4.-) ; Serine Endopeptidases (EC 3.4.21.-) ; TMPRSS2 protein, human (EC 3.4.21.-) ; TMPRSS2 protein, mouse (EC 3.4.21.-) ; virus activating protease (EC 3.4.21.-)
Language	English
Publishing date	2021-07-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00906-21
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Article ; Online: Transcriptome profiling and protease inhibition experiments identify proteases that activate H3N2 influenza A and influenza B viruses in murine airways.

Harbig, Anne / Mernberger, Marco / Bittel, Linda / Pleschka, Stephan / Schughart, Klaus / Steinmetzer, Torsten / Stiewe, Thorsten / Nist, Andrea / Böttcher-Friebertshäuser, Eva

295 ; 33 ; 11388 ; 11407 ; The Journal of biological chemistry ; United States

2020

Abstract	Cleavage of influenza virus hemagglutinin (HA) by host proteases is essential for virus infectivity. HA of most influenza A and B (IAV/IBV) viruses is cleaved at a monobasic motif by trypsin-like proteases. Previous studies have reported that transmembrane serine protease 2 (TMPRSS2) is essential for activation of H7N9 and H1N1pdm IAV in mice but that H3N2 IAV and IBV activation is independent of TMPRSS2 and carried out by as-yet-undetermined protease(s). Here, to identify additional H3 IAV- and IBV-activating proteases, we used RNA-Seq to investigate the protease repertoire of murine lower airway tissues, primary type II alveolar epithelial cells (AECIIs), and the mouse lung cell line MLE-15. Among 13 candidates identified, TMPRSS4, TMPRSS13, hepsin, and prostasin activated H3 and IBV HA in vitro IBV activation and replication was reduced in AECIIs from Tmprss2/Tmprss4-deficient mice compared with WT or Tmprss2-deficient mice, indicating that murine TMPRSS4 is involved in IBV activation. Multicycle replication of H3N2 IAV and IBV in AECIIs of Tmprss2/Tmprss4-deficient mice varied in sensitivity to protease inhibitors, indicating that different, but overlapping, sets of murine proteases facilitate H3 and IBV HA cleavages. Interestingly, human hepsin and prostasin orthologs did not activate H3, but they did activate IBV HA in vitro Our results indicate that TMPRSS4 is an IBV-activating protease in murine AECIIs and suggest that TMPRSS13, hepsin, and prostasin cleave H3 and IBV HA in mice. They further show that hepsin and prostasin orthologs might contribute to the differences observed in TMPRSS2-independent activation of H3 in murine and human airways.
Keywords	TMPRSS2 ; TMPRSS4 ; airway proteases ; cleavage ; hemagglutinin ; hepsin ; host-pathogen interactions ; infectious disease ; influenza virus ; mouse ; mouse lung proteases ; prostasin ; protease gene expression ; serine protease ; trypsin ; trypsin-like protease ; virus
Subject code	570 ; 572
Language	English
Publishing date	2020-04-17
Publisher	Elsevier
Publishing country	de
Document type	Article ; Online
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Article ; Online: Hemagglutinins of avian influenza viruses are proteolytically activated by TMPRSS2 in human and murine airway cells

Bestle, Dorothea / Limburg, Hannah / Kruhl, Diana / Harbig, Anne / Stein, David A. / Moulton, Hong / Matrosovich, Mikhail / Abd el-Whab, El-Sayed Mohammed / Stech, Jürgen / Böttcher-Friebertshäuser, Eva

2021

Abstract	Cleavage of the influenza A virus (IAV) hemagglutinin (HA) by host proteases is indispensable for virus replication. Most IAVs possess a monobasic HA cleavage site cleaved by trypsin-like proteases. Previously, the transmembrane protease TMPRSS2 was shown to be essential for proteolytic activation of IAV HA subtypes H1, H2, H7 and H10 in mice. In contrast, additional proteases are involved in activation of certain H3 IAVs, indicating that HAs with monobasic cleavage site can differ in their sensitivity to host proteases. Here, we investigated the role of TMPRSS2 in proteolytic activation of avian HA subtypes H1 to H11 and H14 to H16 in human and mouse airway cell cultures. Using reassortant viruses carrying representative HAs, we analysed HA cleavage and multicycle replication in (i) lung cells of TMPRSS2-deficient mice and (ii) Calu-3 cells and primary human bronchial cells subjected to morpholino oligomer-mediated knockdown of TMPRSS2 activity. TMPRSS2 was found to be crucial for activation of H1 to H11, H14 and H15 in airway cells of human and mouse. Only H9 with an R-S-S-R cleavage site and H16 were proteolytically activated in the absence of TMPRSS2 activity, albeit with reduced efficiency. Moreover, a TMPRSS2-orthologous protease from duck supported activation of H1 to H11, H15 and H16 in MDCK cells. Together, our data demonstrate that in human and murine respiratory cells, TMPRSS2 is the major activating protease of almost all IAV HA subtypes with monobasic cleavage site. Furthermore, our results suggest that TMPRSS2 supports activation of IAV with monobasic cleavage site in ducks. Importance Human infections with avian influenza A viruses upon exposure to infected birds are frequently reported and have received attention as a potential pandemic threat. Cleavage of the envelope glycoprotein hemagglutinin (HA) by host proteases is a prerequisite for membrane fusion and essential for virus infectivity. In this study, we identify the transmembrane protease TMPRSS2 as the major activating protease of avian ...
Keywords	Text ; ddc:570 ; influenza virus -- TMPRSS2 -- hemagglutinin -- monobasic cleavage site -- virus activating protease -- primary airway cells -- avian influenza -- morpholino oligomers
Subject code	570
Language	English
Publishing date	2021-07-28
Publishing country	de
Document type	Article ; Online
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Article ; Online: TMPRSS2 Is the Major Activating Protease of Influenza A Virus in Primary Human Airway Cells and Influenza B Virus in Human Type II Pneumocytes.

Limburg, Hannah / Harbig, Anne / Bestle, Dorothea / Stein, David A / Moulton, Hong M / Jaeger, Julia / Janga, Harshavardhan / Hardes, Kornelia / Koepke, Janine / Schulte, Leon / Koczulla, Andreas Rembert / Schmeck, Bernd / Klenk, Hans-Dieter / Böttcher-Friebertshäuser, Eva

Journal of virology

2019 Volume 93, Issue 21

Abstract: Cleavage of influenza virus hemagglutinin (HA) by host cell proteases is essential for virus infectivity and spread. We previously ... ...

Abstract	Cleavage of influenza virus hemagglutinin (HA) by host cell proteases is essential for virus infectivity and spread. We previously demonstrated
MeSH term(s)	Animals ; Bronchi/cytology ; Cells, Cultured ; Epithelial Cells/virology ; Gene Knockdown Techniques ; Hemagglutinin Glycoproteins, Influenza Virus/metabolism ; Host-Pathogen Interactions ; Humans ; Influenza A virus/physiology ; Influenza B virus/physiology ; Influenza, Human/enzymology ; Influenza, Human/metabolism ; Influenza, Human/virology ; Mice ; Orthomyxoviridae Infections/enzymology ; Orthomyxoviridae Infections/metabolism ; Orthomyxoviridae Infections/virology ; Pulmonary Alveoli/cytology ; Serine Endopeptidases/genetics ; Serine Endopeptidases/metabolism ; Up-Regulation ; Virus Replication
Chemical Substances	Hemagglutinin Glycoproteins, Influenza Virus ; Serine Endopeptidases (EC 3.4.21.-) ; TMPRSS2 protein, human (EC 3.4.21.-)
Keywords	covid19
Language	English
Publishing date	2019-10-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00649-19
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