Mutation detail:
| Mutation site | F140I |
| Virus | Human respiratory syncytial virus |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | F |
| Gene ID | 1494475 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | P03420.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | Yes |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Fusion protein |
| Uniprot protein ID | P03420 |
| Protein length | 574 amino acids |
| Protein description | F protein is a class I fusion protein composed of 574 amino acids (AA). With a molecular weight of a 50 kDa C-terminal fragment F1 and a 20 kDa N-terminal fragment F2, the protein acquires a trimer of heterodimers. At AA positions 109 and 136, two furin cleavages take place. This feature releases a glycopeptide and thus reveals the hydrophobic site at F1 fragment. F1 and F2 are linked by a cysteine-rich region at two positions: between AA70 and AA212, and between AA37 and AA439. Other Frelated features involve N-glycosylation in F1 at AA position 500, and in F2 at AA positions 27 and 70. F protein is highly conserved, with only 25 AA differences between RSV subtypes A and B. |
Literature information:
| Pubmed ID | 26641933 |
| Clinical information | No |
| Disease | - |
| Published year | 2015 |
| Journal | Nature America |
| Title | Molecular mechanism of respiratory syncytial virus fusion inhibitors |
| Author | Michael B Battles,Johannes P Langedijk,Polina Furmanova-Hollenstein,Supranee Chaiwatpongsakorn,Heather M Costello |
| Evidence | Mutations in any of these three regions may be expected to cause resistance to the fusion inhibitors. Indeed, all of these inhibitors select for escape mutations in the fusion peptide (F140I, L141W, G143S, V144A), in the cysteine-rich region (D392G, K394R |