Mutation detail:
| Mutation site | A789V |
| Virus | Human respiratory syncytial virus |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | L |
| Gene ID | 1494467 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | AY911262.1 |
| Drug/antibody/vaccine | ALS-8112-resistant |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Polymerase |
| Uniprot protein ID | P28887 |
| Protein length | 2165 amino acids |
| Protein description | The core polymerase in RSV is composed of two proteins, a 250 kDa polymerase subunit (L), which contains the RNA-dependent RNA polymerase, the polyribonucleotidyl transferase (PRNTase, capping), and the methyltransferase enzymatic domains essential for viral transcription and replication, and the 27 kDa phosphoprotein (P) accessory protein. . The L protein caps mRNA by a unique RNA-GDP polyribonucleotidyl transferase activity mapped to conserved region V (CRV). Methylation of the cap at the guanine-N-7 and ribose-2-O positions is catalyzed by a unique dual specificity methyltransferase activity that has been functionally mapped to region VI of the L protein. |
Literature information:
| Pubmed ID | 26098424 |
| Clinical information | No |
| Disease | - |
| Published year | 2015 |
| Journal | PLOS PATHOGENS |
| Title | Molecular Basis for the Selective Inhibition of Respiratory Syncytial Virus RNA Polymerase by 2'-Fluoro-4'-Chloromethyl-Cytidine Triphosphate |
| Author | Jerome Deval,Jin Hong,Guangyi Wang,Josh Taylor,Lucas K. Smith |
| Evidence | The four ALS-8112-selected amino acid mutations (QUAD: M628L, A789V, L795I, and I796V) were engineered into the RdRp region of the RSV L gene, and the recombinant L-P protein complex was produced |