作者
Markus Hoffmann, Heike Hofmann-Winkler, Joan C Smith, Nadine Krüger, Prerna Arora, Lambert K Sørensen, Ole S Søgaard, Jørgen Bo Hasselstrøm, Michael Winkler, Tim Hempel, Lluís Raich, Simon Olsson, Olga Danov, Danny Jonigk, Takashi Yamazoe, Katsura Yamatsuta, Hirotaka Mizuno, Stephan Ludwig, Frank Noé, Mads Kjolby, Armin Braun, Jason M Sheltzer, Stefan Pöhlmann
发表日期
2021/3/1
期刊
EBioMedicine
卷号
65
出版商
Elsevier
简介
Background
Antivirals are needed to combat the COVID-19 pandemic, which is caused by SARS-CoV-2. The clinically-proven protease inhibitor Camostat mesylate inhibits SARS-CoV-2 infection by blocking the virus-activating host cell protease TMPRSS2. However, antiviral activity of Camostat mesylate metabolites and potential viral resistance have not been analyzed. Moreover, antiviral activity of Camostat mesylate in human lung tissue remains to be demonstrated.
Methods
We used recombinant TMPRSS2, reporter particles bearing the spike protein of SARS-CoV-2 or authentic SARS-CoV-2 to assess inhibition of TMPRSS2 and viral entry, respectively, by Camostat mesylate and its metabolite GBPA.
Findings
We show that several TMPRSS2-related proteases activate SARS-CoV-2 and that two, TMPRSS11D and TMPRSS13, are robustly expressed in the upper respiratory tract. However, entry mediated by these …
引用总数