Mutation detail:
| Mutation site | V25F |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | E |
| Gene ID | 43740570 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | NC_045512.2 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
decrease |
| Pathogenicity mechanism | Changes associated with the N15A and V25F mutations are suggestive of involvement of E protein N-terminal domain in virus assembly and/or release. |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Envelope Protein |
| Uniprot protein ID | P0DTC4 |
| Protein length | 75 amino acids |
| Protein description | The SARS-CoV-2 envelope (E) protein is a small structural protein involved in many aspects of the viral life cycle. The E protein promotes the packaging and reproduction of the virus, and deletion of this protein weakens or even abolishes the virulence. |
Literature information:
| Pubmed ID | 34003853 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | PLoS Pathogens |
| Title | Interactions of SARS-CoV-2 envelope protein with amilorides correlate with antiviral activity |
| Author | Sang Ho Park, Haley Siddiqi, Daniela V Castro, Anna A De Angelis, Aaron L Oom |
| Evidence | The N15A and V25F mutations in SARS-CoV-2 E protein increased their expression compared to the wild-type protein in HEK293T cell lysates (Fig 9A). Similar to the T16A mutation in IBV E protein, the N15A mutation in SARS-CoV-2 E protein increased VLP production by approximately 40% compared to the wild-type E protein, while the V25F mutation decreased VLP production by 60% compared to wild-type E protein, similar to the effect of the A26F mutation on the IBV E protein (Fig 9B and 9C). |