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Sars-Cov-2 And Betacoronavirus: What Have We Learned In 8 Months?

Agnieszka Kwiatek
Agnieszka Kwiatek
 et 
Monika Adamczyk-Popławska
Monika Adamczyk-Popławska
   | 12 oct. 2020
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Article Category: article
Publié en ligne: 12 oct. 2020
Pages: 197 - 206
Reçu: 01 juin 2020
Accepté: 01 août 2020
DOI: https://doi.org/10.21307/PM-2020.59.3.14
© 2020 Agnieszka Kwiatek et al., published by Sciendo
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Fig. 1.

Scheme illustrating the spike protein of SARS-CoV-2 (A) Scheme of the three-dimensional structure. S1 – S1 subunit, S2 – S2 subunit, RBD – receptor binding domain, TM – transmembrane domain, IC – intracellular tail. The arrows indicate the cleavage site between S1 and S2 subunits; (B) Organization of SARS-CoV-2 spike protein. SP- signal peptide, NTD – N-terminal domain, RBD – receptor binding domain, FP – fusion peptide, IFP – internal fusion peptide, HR1/HR2 – heptad repeat 1/2, TM – transmembrane domain. Arrows indicate the cleavage site S1/S2 and S’; (C) Sequence comparison of the spike proteins of SARS-CoV-2, SARS-CoV and MERS-CoV in a region at S1/S2 boundary. Thin arrows indicate the cleavage site S1/S2 and S’, and wide – the furin cleavage site. The cleavage sites are surrounded by frames. Additionally, site cleaved by furin is grey highlighted. Below the amino acids positions are given.
Scheme illustrating the spike protein of SARS-CoV-2 (A) Scheme of the three-dimensional structure. S1 – S1 subunit, S2 – S2 subunit, RBD – receptor binding domain, TM – transmembrane domain, IC – intracellular tail. The arrows indicate the cleavage site between S1 and S2 subunits; (B) Organization of SARS-CoV-2 spike protein. SP- signal peptide, NTD – N-terminal domain, RBD – receptor binding domain, FP – fusion peptide, IFP – internal fusion peptide, HR1/HR2 – heptad repeat 1/2, TM – transmembrane domain. Arrows indicate the cleavage site S1/S2 and S’; (C) Sequence comparison of the spike proteins of SARS-CoV-2, SARS-CoV and MERS-CoV in a region at S1/S2 boundary. Thin arrows indicate the cleavage site S1/S2 and S’, and wide – the furin cleavage site. The cleavage sites are surrounded by frames. Additionally, site cleaved by furin is grey highlighted. Below the amino acids positions are given.

Functions of Betacoronavirus non-structural proteins

Protein Function
nsp1 Inhibits host translation and gene expression by mRNA degradation and binding 40S ribosome subunit resulting in blocking innate immune response [29, 30, 64].
nsp2 Binds to prohibitin proteins, function not determined [11, 22]
nsp3 PL2pro multi-domain transmembrane protein, possessing:
• ADRP activity, promotes cytokine expression;
• PLPro/Deubiquitinase domain, cleaves viral polyprotein;
• antagonist of IRF3 and NF-τB Signaling resulting in blocking host immune response;
• Ubl1 and Ac domains, interact with N protein;
• Ubl2, NAB, G2M, SUD, Y domains, unknown functions [9, 16, 19, 44, 54].
nsp4 Interacts with nsp3; induce the Formation of Double-Membrane Vesicles [2, 48].
nsp5 MoPro or 3CLpro processing of viral polyproteins [66].
nsp6 Potential transmembrane scaffold protein [40].
nsp7 Forms hexadecameric nsp7-nsp8 complex, essential co-factor of nsp12, may act as processivity clamp for RNA polymerase [34, 77].
nsp8 Forms hexadecameric nsp7-nsp8 complex, essential co-factor of nsp12, may act as primase [34, 77].
nsp9 Single-stranded RNA binding protein [17].
nsp10 Cofactor for nsp16 and nsp14, forms heterodimer with both and stimulates ExoN and S-adenosylmethionine-dependent (nucleoside-2′-O)-methyltransferase [6, 10, 13, 41].
nsp12 RNA-dependent RNA polymerase (RdRp) [34].
nsp13 Superfamily 1-like helicase (HEL1), RNA helicase, 5’ triphosphatase [28].
nsp14 • C-terminal domain functions as a (guanine-N7) methyl transferase (N7-MTase) for mRNA capping.
• N-terminal exoribonuclease (ExoN) domain displays a 3′-5′ exoribonuclease proofreading activity [6, 41].
nsp15 NendoU, uridylate-specific endoribonuclease [78].
nsp16 S-adenosylmethionine-dependent (nucleoside-2′-O)-methyltransferase modifying the RNA cap at ribose 2′-O positions [6, 10].
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Sujets de la revue:
Life Sciences, Microbiology and Virology
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