Mutation detail:
| Mutation site | F49A/M52A/L56A |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | ORF1ab(NSP7) |
| Gene ID | 43740578 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | NC 045512.2 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
decrease |
| Pathogenicity mechanism | Inspection of the crosslinking products of the NSP7-NSP8 mixtures revealed that most of the mutations on the heterodimeric interface I of NSP7 (NSP7F49A and NSP7L56A in Figure3C) and of NSP8 (NSP8F92A in Figure Figure3D) lead to an increased NSP8 dimeriz |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | ORF1ab polyprotein |
| Uniprot protein ID | P0DTC1 |
| Protein length | 7096 amino acids |
| Protein description | ORF1ab, the largest gene, contains overlapping open reading frames that encode polyproteins PP1ab and PP1a. The polyproteins are cleaved to yield 16 nonstructural proteins, NSP1-16. Production of the longer (PP1ab) or shorter protein (PP1a) depends on a -1 ribosomal frameshifting event. The proteins, based on similarity to other coronaviruses, include the papain-like proteinase protein (NSP3), 3C-like proteinase (NSP5), RNA-dependent RNA polymerase (NSP12, RdRp), helicase (NSP13, HEL), endoRNAse (NSP15), 2'-O-Ribose-Methyltransferase (NSP16) and other nonstructural proteins. SARS-CoV-2 nonstructural proteins are responsible for viral transcription, replication, proteolytic processing, suppression of host immune responses and suppression of host gene expression. The RNA-dependent RNA polymerase is a target of antiviral therapies. |
Literature information:
| Pubmed ID | 33999154 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | NUCLEIC ACIDS RESEARCH |
| Title | Two conserved oligomer interfaces of NSP7 and NSP8 underpin the dynamic assembly of SARS-CoV-2 RdRP |
| Author | Mahamaya Biswal, Stephen Diggs, Duo Xu, Nelli Khudaverdyan, Jiuwei Lu |
| Evidence | In contrast, NSP12 alone or any pairwise combination of NSP7, NSP8 and NSP12 fails to generate an appreciable level of RNA product (Figure5B), consistent with previous observations that the co-presence of NSP7 and NSP8 greatly boosts the RNA replication efficiency of NSP12-mediated RNA replication (6,10). Second, introduction of the mutations on the interface I of NSP7 (F49A: NSP7F49A, M52A: NSP7M52A, L56A: NSP7L56A and F49A/M52A/L56A: TM) or NSP8 (F92A: NSP8F92A) lead to a decrease of RdRP efficiency to various extents, with the NSP7 F49A/M52A/L56A triple mutation giving rise to a stronger effect than individual mutations (Figure5C), in line with the impairments of the RdRP assembly by these mutations. |