Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry.

By G. Simmons, D. Gosalia, Andrew J Rennekamp, J. Reeves, S. Diamond, P. Bates. Proceedings of the National Academy of Sciences of the United States of America, 2005

1,063 citations recorded by the source corpus.

Subfields: Infectious Diseases, Molecular Biology, Public Health, Environmental and Occupational Health

View Paper: https://www.semanticscholar.org/paper/7e3f4303517b9c4b96848eb3f1f3aff144481446

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Citations in the corpus

SARS coronavirus entry into host cells through a novel clathrin- and caveolae-independent endocytic pathway (2008, background): “Some later studies have shown that entry of SARS-CoV may be pH-dependent [12] , and that the endosomal protease cathepsin L [13, 14] might be involved, suggesting that this virus may employ endocytosis.”
Coronavirus Pathogenesis (2011, background): “2 below, several different proteases, including cathepsin L (Simmons et al., 2005) and the serine protease TMPRSS2 (Matsuyama et al.”
Host cell proteases: critical determinants of coronavirus tropism and pathogenesis (2014, background): “…of virus entry on low-pH was because ARS-CoV S can be activated by endosomal cathepsin L, which equires low pH for its enzymatic activity (Simmons et al., 2005). urprisingly, SARS-CoV seems to have evolved a multi-pronged pproach regarding the activation of its S as many other proeases…”
Mechanisms of Coronavirus Cell Entry Mediated by the Viral Spike Protein (2012, background): “It has been shown that SARS-CoV infection is inhibited by lysomotropic agents because of the inhibition of the low-pH-actived protease cathepsin L [72] .”
SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor (2020, background): “The S proteins of SARS-CoV can use the endosomal cysteine proteases CatB/L for S protein priming in TMPRSS2 cells (Simmons et al., 2005).”
Distinct Patterns of IFITM-Mediated Restriction of Filoviruses, SARS Coronavirus, and Influenza A Virus (2011, background): “Previous studies have shown that the cathepsin L dependence of SARS-CoV can be bypassed by addition of exogenous trypsin to ACE2-bound virions or pseudovirions, likely by inducing Sprotein-mediated fusion at or near the plasma membrane [11,16].”
Structural insights into coronavirus entry (2019, background): “…activity and/or virus entry into host cells using experiments of inhibition of intracellular proteases (Burkard et al., 2014; Frana et al., 1985; Simmons et al., 2005; Yamada and Liu, 2009) and/or substitutions of residues at the S1/S2 or S2’ cleavage sites (Belouzard et al., 2009; Li et al.,…”
A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells (2020, neutral): “A cathepsin B/L-dependent auxiliary activation pathway is operative in many TMPRSS2 cell lines but seems not to be available in viral target cells in the lung because TMPRSS2dependent activation of the S protein is essential for robust MERS-CoV and SARS-CoV spread and pathogenesis in the infected ho”
Human Coronavirus: Host-Pathogen Interaction. (2019, background): “For instance, activation of SARS-CoV S protein requires sequential cleavage by the endosomal cysteine protease cathepsin L (7, 105) and another trypsin-like serine protease (4).”
Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme (2008, background): “…Hendra and Nipah virus F, post synthetic cleavage by extracellular or intracellular (e.g., endosomal cathepsins) proteases may substitute (Chandran et al., 2005; Follis et al., 2006; Matsuyama et al., 2005; Pager et al., 2006; Pager and Dutch, 2005; Schornberg et al., 2006; Simmons et al., 2005).”
The origin, transmission and clinical therapies on coronavirus disease 2019 (COVID-19) outbreak – an update on the status (2020, background): “mer S protein is triggered by the cell surface-associated transmembrane protease serine 2 (TMPRSS2) [39] and cathepsin [40], while the possible molecules facilitated membrane invagination for SARS-CoV-2 endocytosis are still unclear.”
Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites (2009, background): “Analysis of both SARS-CoV infection and transduction by SARS-CoV S-pseudotyped virions has indicated that the virus is sensitive to inhibitors of endosomal acidification (13–17), and it has been shown that SARS-CoV S-pseudotyped virions use the endosomal protease cathepsin L to infect cells (18, 19)”