Id |
Subject |
Object |
Predicate |
Lexical cue |
T115 |
0-151 |
Sentence |
denotes |
CoVs, like other positive-stranded RNA viruses, induce membranous rearrangements of varying morphologies that are essential for RTCs anchoring [82,83]. |
T116 |
152-401 |
Sentence |
denotes |
The CoV-induced replicative structures consist of double-membrane vesicles (DMVs) and convoluted membranes (CMs), which form a large reticulovesicular network that are critical for viral replication and transcription [84,85,86,87,88,89,90,91,92,93]. |
T117 |
402-568 |
Sentence |
denotes |
Among the CoV nsps, nsp3, nsp4, and nsp6 include the hydrophobic transmembrane domains engaging in anchoring the viral RNA synthesis components to the membranes [94]. |
T118 |
569-659 |
Sentence |
denotes |
For MERS-CoV and SARS-CoV, co-expression of nsp3 and nsp4 is required to induce DMVs [95]. |
T119 |
660-764 |
Sentence |
denotes |
SARS-CoV nsp6 has membrane proliferation ability as well, which also contributes to DMVs formation [96]. |
T120 |
765-832 |
Sentence |
denotes |
The structure and functions of α-CoV nsp3 are largely unknown [97]. |
T121 |
833-1093 |
Sentence |
denotes |
Nsp4 is also a marker for CoV-induced membrane structures; some results indicate that the nsp4–10 of pp1a act as a large complex through multidomain structure or scaffold during viral RNA replication progress, before its cleavage into individual products [98]. |
T122 |
1094-1142 |
Sentence |
denotes |
CoVs nsp5 encodes a 3C-like proteinase (3CLpro). |
T123 |
1143-1261 |
Sentence |
denotes |
The polyproteins pp1a and pp1ab are processed into individual elements of replicase by 3C-like protease and PLPs [99]. |
T124 |
1262-1375 |
Sentence |
denotes |
Moreover, PEDV nsp5 plays a crucial role in virus replication and also blocks host innate immune responses [100]. |
T125 |
1376-1587 |
Sentence |
denotes |
Crystallographic or nuclear magnetic resonance structures have shown that nsp3, nsp5, nsp7, nsp8, nsp9, and nsp10 have the PLprob and the ADP-ribose 1′′-phosphatase (ADRP) activity [101,102,103,104,105,106,107]. |
T126 |
1588-1709 |
Sentence |
denotes |
The crystal structure of SARS-CoV nsp9 suggests that nsp9 is dimeric and it is able to bind to single-stranded RNA [108]. |
T127 |
1710-1855 |
Sentence |
denotes |
The crystal structure of SARS CoV nsp10 protein suggests that nsp10 is a zinc-finger protein, which is existent exclusively in CoVs so far [107]. |
T128 |
1856-1963 |
Sentence |
denotes |
Moreover, nsp7–10 have RNA binding activity and nsp12 encodes a single RNA-dependent RNA polymerase (RdRp). |
T129 |
1964-2130 |
Sentence |
denotes |
The biochemical characterization and crystallization of SARS CoV nsp7 and nsp8 manifests that eight copies of nsp8 and eight copies of nsp7 form a supercomplex [106]. |
T130 |
2131-2250 |
Sentence |
denotes |
The complex is supportive for nucleic acid binding and may be associated with the processivity of viral RdRp [102,106]. |
T131 |
2251-2433 |
Sentence |
denotes |
Recently, structural studies have described that the SARS-CoV nsp12 polymerase binds to the nsp7 and nsp8 complex [109] that may increase the polymerase activity of nsp12 RdRp [110]. |
T132 |
2434-2534 |
Sentence |
denotes |
CoV nsp13, a NTPase/helicase, is also determined to play essential roles in viral replication [111]. |
T133 |
2535-2663 |
Sentence |
denotes |
CoV nsp14 is a multifunctional protein with 3′-5′ exoribonuclease activity and N-7-methyltransferase [MTase] activity [112,113]. |
T134 |
2664-2737 |
Sentence |
denotes |
Nsp14 catalyzes the N7-methylation of Gppp-RNA to form a cap-0 structure. |
T135 |
2738-2851 |
Sentence |
denotes |
CoV nsp15 encodes an endoribonuclease (EndoU), performing functions through a hexamer in many CoVs [114,115,116]. |
T136 |
2852-2938 |
Sentence |
denotes |
The endoribonuclease activity of nsp15 is not essential for CoV replication [117,118]. |
T137 |
2939-3192 |
Sentence |
denotes |
For CoVs, the 5′ end of the viral genomic RNA and subgenomic mRNA (sgmRNA) is supposed to have cap structures: an N-7 methylated guanosine nucleoside (m7GpppN) (cap 0) and a methyl group at the 2′-O-ribose position (cap 1) of the first nucleotide [119]. |
T138 |
3193-3401 |
Sentence |
denotes |
These cap structures enhance the initiation of translation of viral proteins, protect viral mRNAs against cellular 5′-3′-exoribonuclease and limit the recognition of viral RNA by host innate system [120,121]. |
T139 |
3402-3494 |
Sentence |
denotes |
Nsp13 is proposed to catalyze the first step of the 5′-capping reaction of viral RNAs [122]. |
T140 |
3495-3662 |
Sentence |
denotes |
The methylation of the two sites in the 5′ cap are catalyzed by three nsps; nsp14 (the N-7-MTase), nsp16 (the 2′-O-methyltransferase), and nsp10 [112,123,124,125,126]. |
T141 |
3663-3846 |
Sentence |
denotes |
In addition, the 3′-5′ exoribonuclease activity of nsp14 is involved in a replicative mismatch repair system during RNA synthesis, which improves the replication fidelity of CoV [42]. |
T142 |
3847-4096 |
Sentence |
denotes |
Although these nsps have been demonstrated to play essential roles in viral replication, transcription and/or post-translational polyprotein processing [127], the nsp12–16 of PEDV and other CoVs are poorly characterized to date, except for SARS-CoV. |