Mutation detail:
| Mutation site | R75A |
| 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 | - |
| 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 addition, we investigated the RdRP complex carrying mutations on the potential RNA binding sites of NSP8, including K58A (NSP8K58A), R75A (NSP8R75A) and K82A (NSP8K82A) located on the N-terminal domain. Structural studies of the SARS-CoV-2 NSP7-NSP8-NSP12 complexes with RNA substrate bound (6,8,10,22) revealed that these residues are positioned in close proximity to the backbone of the exiting RNA duplex (Supplementary Figure S6). Indeed, all three mutations lead to a significant reduction of the RdRP efficiency (Figure (Figure5E),5E), confirming the important role of these residues in regulating the RdRP activity. |