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TMPRSS2 / Epitheliasin

transmembrane protease, serine 2

Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus-cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike glycoprotein which activates the glycoprotein for cathepsin L-independent host cell entry. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) , human coronavirus EMC (HCoV-EMC), SARS-CoV and SARS-CoV-2, and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Gene Name: transmembrane protease, serine 2
Family/Subfamily: Protease , Serine S1
Synonyms: TMPRSS2, Epitheliasin, PRSS10, Serine protease 10, PP9284, host protease for SARS-CoV-2 replication
Target Sequences: NM_005656 NP_005647.3 O15393

Publications (4)

1
Camostat mesylate inhibits SARS-CoV-2 activation by TMPRSS2-related proteases and its metabolite GBPA exerts antiviral activity10<sup> Fraunhofer Institute for Toxicology and Experimental Medicine ITEM, Biomedical Research in Endstage and Obstructive Lung Disease Hannover (BREATH), Member of the German Center for Lung Research (DZL), Member of Fraunhofer International Consortium for Anti-Infective Research (iCAIR), Nikolai-Fuchs-Strasse 1, 30625 Hannover, Germany12<sup> Discovery Technology Rese. 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. EBioMedicine. 2021 Mar;;65:103255. [Full Text Article] [PubMed:33676899] [PMC:PMC7930809]
2
Coagulation factors directly cleave SARS-CoV-2 spike and enhance viral entry. bioRxiv : the preprint server for biology. 2021 Jul; [Full Text Article] [PubMed:33821268] [PMC:PMC8020968]
3
Synergistic inhibition of SARS-CoV-2 cell entry by otamixaban and covalent protease inhibitors: pre-clinical assessment of pharmacological and molecular properties. Tim Hempel , Katarina Elez, Nadine Krüger, Lluís Raich, Jonathan H Shrimp, Olga Danov, Danny Jonigk , Armin Braun, Min Shen, Matthew D Hall, Stefan Pöhlmann , Markus Hoffmann , Frank Noé. Chemical science. 2021 Aug;12:12600-12609. [Full Text Article] [PubMed:34703545] [PMC:PMC8494051]
4
Identification of trypsin-degrading commensals in the large intestine. Youxian Li , Eiichiro Watanabe , Yusuke Kawashima , Damian R Plichta, Zhujun Wang, Makoto Ujike, Qi Yan Ang, Runrun Wu, Munehiro Furuichi, Kozue Takeshita, Koji Yoshida, Keita Nishiyama, Sean M Kearney, Wataru Suda, Masahira Hattori, Satoshi Sasajima, Takahiro Matsunaga, Xiaoxi Zhang, Kazuto Watanabe, Jun Fujishiro, Jason M Norman, Bernat Olle, Shutoku Matsuyama, Ho Namkoong, Yoshifumi Uwamino, Makoto Ishii, Koichi Fukunaga, Naoki Hasegawa, Osamu Ohara, Ramnik J Xavier, Koji Atarashi, Kenya Hond. Nature. 2022 September;609:582-589. [Full Text Article] [PubMed:36071157] [PMC:PMC9477747] Related Antibodies: LS-C373022.
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The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).