Mutation detail:
| Mutation site | M141V |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | ORF1ab(NSP2) |
| Gene ID | 43740578 |
| Country | China(Hong Kong) |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | GH |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | MT644268.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| 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 | 33900193 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | EMERGING INFECTIOUS DISEASES |
| Title | Introduction of ORF3a-Q57H SARS-CoV-2 Variant Causing Fourth Epidemic Wave of COVID-19, Hong Kong, China |
| Author | Daniel K.W. Chu, Kenrie P.Y. Hui, Haogao Gu, Ronald L.W. Ko, Pavithra Krishnan |
| Evidence | Our full genome analysis revealed that the wave 4 virus has several nonsilent mutations associated with host adaptation (4-6; B. Zhou et al., unpub. data, https://doi.org/10.1101/2020.10.27.357558), including mutations in the RNA-dependent RNA polymerase (RdRp[L323P]), Spike(D614G), open reading frame 3a (ORF3a[Q57H]), ORF3b(E14*), and nucleocapsid (N[S194L]) proteins. The ORF3a(Q57H) mutation leads a major truncation of ORF3b protein, ORF3b(E14*) (6). |