Publications by authors named "Marie Schwerdtner"

Article Synopsis
  • The zoonotic transmission of influenza A viruses (IAVs) and coronaviruses (CoVs) can lead to severe diseases, and the cleavage of glycoproteins is essential for their infectivity.
  • The study focused on the role of transmembrane serine protease 2 (TMPRSS2) in cleaving viral proteins in human airway cells and its dependency for different IAV and CoV strains.
  • Results showed that while TMPRSS2 is crucial for the activation of certain viruses like H1N1/1918 and MERS-CoV, others like SARS-CoV and some IAV subtypes show less dependency, indicating the potential for alternative proteases and highlighting TMPRSS2 as
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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.

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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.

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Many viruses require proteolytic activation of their envelope proteins for infectivity, and relevant host proteases provide promising drug targets. The transmembrane serine protease 2 (TMPRSS2) has been identified as a major activating protease of influenza A virus (IAV) and various coronaviruses (CoV). Increased TMPRSS2 expression has been associated with a higher risk of severe influenza infection and enhanced susceptibility to SARS-CoV-2.

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Background: The transmembrane protease serine 2 (TMPRSS2) proteolytically activates the envelope proteins of several viruses for viral entry via membrane fusion and is therefore an interesting and promising target for the development of broad-spectrum antivirals. However, the use of a host protein as a target may lead to potential side effects, especially on the immune system. We examined the effect of a genetic deletion of on dendritic cells.

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