Mutation detail:
| Mutation site | 4829A>G |
| Virus | Human respiratory syncytial virus |
Mutation level  |
Nucleotide 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 | 15567433 |
| Clinical information | No |
| Disease | - |
| Published year | 2004 |
| Journal | Virology |
| Title | Respiratory syncytial virus deficient in soluble G protein induced an increased proinflammatory response in human lung epithelial cells |
| Author | Ralf Arnold, Brigitte Kfnig, Hermann Werchau, Wolfgang Kfnig |
| Evidence | The isolated mutant (7th passage) possess a point mutation in the G gene at position 157 (A to G), which led to an exchange at amino acid 48 from methionine to valine and therefore in an inactivation of the second start codon in the ORF of the G gene. |