Mutation detail:
| Mutation site | L4169F |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | ORF1ab(NSP9) |
| Gene ID | 43740578 |
| Country | Vietnam |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
Human |
| Variants | Alpha |
| Viral reference sequence | NC_045512.2 |
| 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 | 33647228 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | EMERGING INFECTIOUS DISEASES |
| Title | Novel Mutation of SARS-CoV-2, Vietnam, July 2020 |
| Author | Hoang Vu Mai Phuong,Trinh Son Tung,Ung Thi Hong Trang,Nguyen Le Khanh Hang,Nguyen Vu Son |
| Evidence | A novel SNP at position 12772 (A>C) was found in all 26 sequences; it represents a nonsynonymous mutation in nonstructural protein 9 resulting in a leucine to phenylalanine change at amino acid site 4169 in open reading frame 1ab. |