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10.1080/22221751.2020.1870414

http://scihub22266oqcxt.onion/10.1080/22221751.2020.1870414
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suck abstract from ncbi


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pmid33372854      Emerg+Microbes+Infect 2021 ; 10 (1): 178-195
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  • SARS-CoV-2 proteases PLpro and 3CLpro cleave IRF3 and critical modulators of inflammatory pathways (NLRP12 and TAB1): implications for disease presentation across species #MMPMID33372854
  • Moustaqil M; Ollivier E; Chiu HP; Van Tol S; Rudolffi-Soto P; Stevens C; Bhumkar A; Hunter DJB; Freiberg AN; Jacques D; Lee B; Sierecki E; Gambin Y
  • Emerg Microbes Infect 2021[Dec]; 10 (1): 178-195 PMID33372854show ga
  • The genome of SARS-CoV-2 encodes two viral proteases (NSP3/papain-like protease and NSP5/3C-like protease) that are responsible for cleaving viral polyproteins during replication. Here, we discovered new functions of the NSP3 and NSP5 proteases of SARS-CoV-2, demonstrating that they could directly cleave proteins involved in the host innate immune response. We identified 3 proteins that were specifically and selectively cleaved by NSP3 or NSP5: IRF-3, and NLRP12 and TAB1, respectively. Direct cleavage of IRF3 by NSP3 could explain the blunted Type-I IFN response seen during SARS-CoV-2 infections while NSP5 mediated cleavage of NLRP12 and TAB1 point to a molecular mechanism for enhanced production of cytokines and inflammatory responThe genome of SARS-CoV-2 encodes two viral proteases (NSP3/papain-like protease and NSP5/3C-like protease) that are responsible for cleaving viral polyproteins during replication. Here, we discovered new functions of the NSP3 and NSP5 proteases of SARS-CoV-2, demonstrating that they could directly cleave proteins involved in the host innate immune response. We identified 3 proteins that were specifically and selectively cleaved by NSP3 or NSP5: IRF-3, and NLRP12 and TAB1, respectively. Direct cleavage of IRF3 by NSP3 could explain the blunted Type-I IFN response seen during SARS-CoV-2 infections while NSP5 mediated cleavage of NLRP12 and TAB1 point to a molecular mechanism for enhanced production of cytokines and inflammatory response observed in COVID-19 patients. We demonstrate that in the mouse NLRP12 protein, one of the recognition site is not cleaved in our in-vitro assay. We pushed this comparative alignment of IRF-3 and NLRP12 homologs and show that the lack or presence of cognate cleavage motifs in IRF-3 and NLRP12 could contribute to the presentation of disease in cats and tigers, for example. Our findings provide an explanatory framework for indepth studies into the pathophysiology of COVID-19.
  • |Adaptor Proteins, Signal Transducing/*metabolism[MESH]
  • |Amino Acid Sequence[MESH]
  • |Animals[MESH]
  • |COVID-19/pathology[MESH]
  • |Cell Line[MESH]
  • |Chiroptera/virology[MESH]
  • |Coronavirus 3C Proteases/genetics/*metabolism[MESH]
  • |Coronavirus Papain-Like Proteases/genetics/*metabolism[MESH]
  • |HEK293 Cells[MESH]
  • |Humans[MESH]
  • |Interferon Regulatory Factor-3/*metabolism[MESH]
  • |Intracellular Signaling Peptides and Proteins/*metabolism[MESH]
  • |Mice[MESH]


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