Mutation detail:
Mutation site | L208A |
Virus | Human respiratory syncytial virus |
Mutation level ![]() |
Amino acid Level |
Gene/protein/region type | G |
Gene ID | 1494474 |
Country | - |
Mutation type ![]() |
nonsynonymous mutation |
Genotype/subtype/clade | - |
Sample ![]() |
cell line |
Variants | - |
Viral reference sequence | M74568.1 |
Drug/antibody/vaccine | - |
Transmissibility ![]() |
- |
Transmission mechanism | - |
Pathogenicity ![]() |
- |
Pathogenicity mechanism | - |
Immune escape mutation | - |
Immune escape mechanism | - |
RT-PCR primers probes | - |
Protein detail:
Protein name | Attachment glycoprotein |
Uniprot protein ID | P03423 |
Protein length | 298 amino acids |
Protein description | G protein is another target for neutralizing antibodies and it is a type II integral membrane protein composed of 298AA and weights ~ 90 kDa. It is vastly glycosylated and it is expressed in secreted and membrane-anchored forms called Gs and Gm, respectively. Gs is linked to neutralization inhibition, while Gm is related to viral attachment. This hostvirus membrane attachment is mediated by heparin sulfate proteoglycans receptor interaction. The antigenic variation is situated in the mucin domain of G protein at both C- and N- terminal ends. N- and O-glycosylation enables the protein to mature and enhances immune escape mechanisms. Other feature includes a central conserved region (CX3C motif) which is responsible for CX3CR1 binding to diminish inflammatory cytokines release. |
Literature information:
Pubmed ID | 26581976 |
Clinical information | No |
Disease | - |
Published year | 2016 |
Journal | Journal of virology |
Title | Preventing Cleavage of the Respiratory Syncytial Virus Attachment Protein in Vero Cells Rescues the Infectivity of Progeny Virus for Primary Human Airway Cultures |
Author | Jacqueline Corry,Sara M. Johnson,Jessica Cornwell,Mark E. Peeples |
Evidence | All viruses were titrated on HeLa cells. HeLa or Vero cells were inoculated with rgRSV or rgRSV with the L208A mutation (rgRSV-L208A) as described above. |