Mutation detail:
Mutation site | S190F |
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 ![]() |
Human |
Variants | - |
Viral reference sequence | KT992094.1 |
Drug/antibody/vaccine | - |
Transmissibility ![]() |
- |
Transmission mechanism | - |
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 | 28835504 |
Clinical information | No |
Disease | - |
Published year | 2017 |
Journal | Journal of virology |
Title | Attenuated Human Parainfluenza Virus Type 1 Expressing the Respiratory Syncytial Virus (RSV) Fusion (F) Glycoprotein from an Added Gene: Effects of Prefusion Stabilization and Packaging of RSV F |
Author | Xiang Liu,Bo Liang,Joan Ngwuta,Xueqiao Liu,Sonja Surman |
Evidence | McLellan and coworkers previously described increasing RSV pre-F stability by the introduction of disulfide bond (DS), generating mutations (S155C and S290C), as well as the further introduction of hydrophobic cavity-filling (Cav1) substitutions (S190F an |