Truncated reactive center loop decrease the inhibitory activity of Antheraea pernyi serine protease inhibitor 6

2020 ◽  
Vol 105 (1) ◽  
Author(s):  
Guobao Wang ◽  
Shuang Na ◽  
Li Qin
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Inhibitory Activity ◽  
Serine Protease Inhibitor ◽  
Antheraea Pernyi ◽  
Reactive Center Loop ◽  
Reactive Center

scholarly journals Alpha 1 Antitrypsin is an Inhibitor of the SARS-CoV-2–Priming Protease TMPRSS2

2021 ◽  
Vol 6 (1) ◽  
pp. 55-74
Author(s):  
Nurit P Azouz ◽  
Andrea Klingler ◽  
Victoria Callahan ◽  
Ivan Akhrymuk ◽  
Katarina Elez ◽  
...  
Keyword(s):  
Viral Load ◽  
Protease Inhibitor ◽  
Serine Protease ◽  
Inhibitory Activity ◽  
Serine Proteases ◽  
Serine Protease Inhibitor ◽  
Host Cells ◽  
S Protein ◽  
Relative Contribution ◽  
Alpha 1 Antitrypsin

Background: Host proteases have been suggested to be crucial for dissemination of MERS, SARS-CoV, and SARS-CoV-2 coronaviruses, but the relative contribution of membrane versus intracellular proteases remains controversial. Transmembrane serine protease 2 (TMPRSS2) is regarded as one of the main proteases implicated in the coronavirus S protein priming, an important step for binding of the S protein to the angiotensin-converting enzyme 2 (ACE2) receptor before cell entry.  Methods: We developed a cell-based assay to identify TMPRSS2 inhibitors. Inhibitory activity was established in SARS-CoV-2 viral load systems. Results: We identified the human extracellular serine protease inhibitor (serpin) alpha 1 antitrypsin (A1AT) as a novel TMPRSS2 inhibitor. Structural modeling revealed that A1AT docked to an extracellular domain of TMPRSS2 in a conformation that is suitable for catalysis, resembling similar serine protease inhibitor complexes. Inhibitory activity of A1AT was established in a SARS-CoV-2 viral load system. Notably, plasma A1AT levels were associated with COVID-19 disease severity.  Conclusions: Our data support the key role of extracellular serine proteases in SARS CoV-2 infections and indicate that treatment with serpins, particularly the FDA-approved drug A1AT, may be effective in limiting SARS-CoV-2 dissemination by affecting the surface of the host cells.

Novel Inhibitory Activity for Serine Protease Inhibitor Kazal Type-3 (Spink3) on Human Recombinant Kallikreins

2013 ◽  
Vol 20 (10) ◽  
pp. 1098-1107 ◽  
Author(s):  
Diego Assis ◽  
Lucia Zalazar ◽  
Maria Juliano ◽  
Rosana Castro ◽  
Andreina Cesari
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Inhibitory Activity ◽  
Serine Protease Inhibitor ◽  
Type 3

A serine protease inhibitor from Musca domestica larva exhibits inhibitory activity against elastase and chymotrypsin

2016 ◽  
Vol 38 (7) ◽  
pp. 1147-1153 ◽  
Author(s):  
Yan Tang ◽  
Ying Wang ◽  
Zhihuan Pei ◽  
Wenting Li ◽  
Dandan Zhang ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Musca Domestica ◽  
Inhibitory Activity ◽  
Serine Protease Inhibitor

scholarly journals Extending the Cellulosome Paradigm: the Modular Clostridium thermocellum Cellulosomal Serpin PinA Is a Broad-Spectrum Inhibitor of Subtilisin-Like Proteases

2013 ◽  
Vol 79 (19) ◽  
pp. 6173-6175 ◽  
Author(s):  
Páraic Ó Cuív ◽  
Rajesh Gupta ◽  
Hareshwar P. Goswami ◽  
Mark Morrison
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Broad Spectrum ◽  
Inhibitory Activity ◽  
Clostridium Thermocellum ◽  
Serine Protease Inhibitor ◽  
Content Type

ABSTRACTClostridium thermocellumencodes a cellulosomal, modular, and thermostable serine protease inhibitor (serpin), PinA. PinA stability but not inhibitory activity is affected by the Fn(III) and Doc(I) domains, and PinA is a broad inhibitor of subtilisin-like proteases and may play a key role in protecting the cellulosome from protease attack.

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