Mutation detail:
| Mutation site | S275F |
| 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 | A |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | M74568.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
promote |
| Transmission mechanism | Mutations of residues K272 and S275 (K272M, K272N, K272Q, K272T, and S275F) reduced palivizumab binding as expected based upon previous studies [11-14,24], yet retained binding by MAb19 and ch101F confirming that MAb19 and ch101F recognize a different epi |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| 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 | 17623075 |
| Clinical information | No |
| Disease | - |
| Published year | 2007 |
| Journal | Virology Journal |
| Title | Relationship between the loss of neutralizing antibody binding and fusion activity of the F protein of human respiratory syncytial virus |
| Author | Changbao Liu, Nicole D Day, Patrick J Branigan, Lester L Gutshall, Robert T Sarisky |
| Evidence | Table 1 |