Mutation detail:
| Mutation site | S215R |
| Virus | Human rhinovirus |
Mutation level  |
Amino acid level |
| Gene/protein/region type | VP1 |
| Gene ID | 5758809 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | C |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | GU219984.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Capsid Protein VP1 |
| Uniprot protein ID | A0A2P1DXU1 |
| Protein length | 274 amino acids |
| Protein description | Capsid protein VP1 forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks. |
Literature information:
| Pubmed ID | 27743961 |
| Clinical information | No |
| Disease | - |
| Published year | 2016 |
| Journal | Virology |
| Title | Mutations in VP1 and 3A proteins improve binding and replication of rhinovirus C15 in HeLa-E8 cells |
| Author | Yury A Bochkov,Kelly Watters,Sarmila Basnet,Shakher Sijapati,Marchel Hill |
| Evidence | Figure2 |