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Tytuł:
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Spatial and temporal roles of SARS-CoV PL -A snapshot.
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Autorzy:
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Yan S; National Engineering Research Center for Non-Food Biorefinery, State Key Laboratory of Non-Food Biomass and Enzyme Technology, Guangxi Biomass Engineering Technology Research Center, Guangxi Key Laboratory of Bio-Refinery, Guangxi Academy of Sciences, Nanning, China.
Wu G; National Engineering Research Center for Non-Food Biorefinery, State Key Laboratory of Non-Food Biomass and Enzyme Technology, Guangxi Biomass Engineering Technology Research Center, Guangxi Key Laboratory of Bio-Refinery, Guangxi Academy of Sciences, Nanning, China.
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Źródło:
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FASEB journal : official publication of the Federation of American Societies for Experimental Biology [FASEB J] 2021 Jan; Vol. 35 (1), pp. e21197.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't; Review
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Język:
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English
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Imprint Name(s):
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Publication: 2020- : [Bethesda, Md.] : Hoboken, NJ : Federation of American Societies for Experimental Biology ; Wiley
Original Publication: [Bethesda, Md.] : The Federation, [c1987-
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MeSH Terms:
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COVID-19/*virology
Coronavirus Papain-Like Proteases/*physiology
Severe acute respiratory syndrome-related coronavirus/*physiology
SARS-CoV-2/*physiology
Severe Acute Respiratory Syndrome/*virology
COVID-19/immunology ; COVID-19/therapy ; Coronavirus Papain-Like Proteases/genetics ; Genes, Viral ; Host-Pathogen Interactions ; Humans ; Molecular Targeted Therapy ; NF-kappa B/metabolism ; Protein Domains ; Protein Processing, Post-Translational ; Severe acute respiratory syndrome-related coronavirus/genetics ; SARS-CoV-2/genetics ; Severe Acute Respiratory Syndrome/immunology ; Severe Acute Respiratory Syndrome/therapy ; Substrate Specificity ; Ubiquitin-Activating Enzymes/metabolism ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination ; Viral Proteins/metabolism ; Virus Replication
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References:
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Grant Information:
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AB17190534 International Key Project of Guangxi Scienticfic Research and Tecknology Development Plan; 31560315 International National Natural Science Foundation of China (NSFC)
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Contributed Indexing:
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Keywords: ISG15; PLpro; SARS-CoV; SARS-CoV-2; p53; ubiquitin
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Substance Nomenclature:
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0 (NF-kappa B)
0 (Viral Proteins)
EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes)
EC 2.3.2.27 (Ubiquitin-Protein Ligases)
EC 3.4.22.2 (Coronavirus Papain-Like Proteases)
EC 3.4.22.2 (papain-like protease, SARS coronavirus)
EC 3.4.22.2 (papain-like protease, SARS-CoV-2)
EC 6.2.1.45 (Ubiquitin-Activating Enzymes)
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Entry Date(s):
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Date Created: 20201228 Date Completed: 20210111 Latest Revision: 20221207
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Update Code:
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20240105
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PubMed Central ID:
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PMC7883198
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DOI:
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10.1096/fj.202002271
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PMID:
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33368679
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SARS-CoV and SARS-CoV-2 encode four structural and accessory proteins (spike, envelope, membrane and nucleocapsid proteins) and two polyproteins (pp1a and pp1ab). The polyproteins are further cleaved by 3C-like cysteine protease (3CL pro ) and papain-like protease (PL pro ) into 16 nonstructural proteins (nsps). PL pro is released from nsp3 through autocleavage, and then it cleaves the sites between nsp1/2, between nsp2/3 and between nsp3/4 with recognition motif of LXGG, and the sites in the C-terminus of ubiquitin and of protein interferon-stimulated gene 15 (ISG15) with recognition motif of RLRGG. Alone or together with SARS unique domain (SUD), PL pro can stabilize an E3 ubiquitin ligase, the ring-finger, and CHY zinc-finger domain-containing 1 (RCHY1), through domain interaction, and thus, promote RCHY1 to ubiquitinate its target proteins including p53. However, a dilemma appears in terms of PL pro roles. On the one hand, the ubiquitination of p53 is good for SARS-CoV because the ubiquitinated p53 cannot inhibit SARS-CoV replication. On the other hand, the ubiquitination of NF-κB inhibitor (IκBα), TNF receptor-associated factors (TRAFs), and stimulator of interferon gene (STING), and the ISGylation of targeted proteins are bad for SARS-CoV because these ubiquitination and ISGylation initiate the innate immune response and antiviral state. This mini-review analyzes the dilemma and provides a snapshot on how the viral PL pro smartly manages its roles to avoid its simultaneously contradictory actions, which could shed lights on possible strategies to deal with SARS-CoV-2 infections.
(© 2020 The Authors. The FASEB Journal published by Wiley Periodicals LLC on behalf of Federation of American Societies for Experimental Biology.)