Mutation detail:
| Mutation site | I109V |
| Virus | Norovirus |
Mutation level  |
Amino acid level |
| Gene/protein/region type | ORF1(3CLpro) |
| Gene ID | 1491970 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | GI, GII, GV |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | M87661.1, DQ658413.1, DQ285629.1 |
| Drug/antibody/vaccine | rupintrivir resistant |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Nonstructural Polyprotein |
| Uniprot protein ID | Q83883 |
| Protein length | 1789 amino acids |
| Protein description | ORF1 encodes six non-structural (NS) proteins involved in viral replication, which are: N-Term (NS1/2), NTPase (NS3), 3C-like (NS4), VPg (NS5), Protease (NS6), and RNA-dependent RNA polymerase (RdRp; NS7). Protein p48 may play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes. NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity. Protein P22 may play a role in targeting replication complex to intracellular membranes. Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation. 3C-like protease processes the polyprotein: 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved. May cleave host polyadenylate-binding protein thereby inhibiting cellular translation. |
Literature information:
| Pubmed ID | 29530860 |
| Clinical information | No |
| Disease | - |
| Published year | 2018 |
| Journal | Antimicrobial Agents and Chemotherapy |
| Title | Selection and Characterization of Rupintrivir-Resistant Norwalk Virus Replicon Cells In Vitro |
| Author | Mitsutaka Kitano, Myra Hosmillo, Edward Emmott, Jia Lu, Ian Goodfellow |
| Evidence | Here we report, for the first time, the generation of rupintrivir-resistant human Norwalk virus replicon cells in vitro Sequence analysis revealed that these replicon cells contained amino acid substitutions of alanine 105 to valine (A105V) and isoleucine |