Mutation detail:
| Mutation site | P230L |
| Virus | Human respiratory syncytial virus |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | G |
| Gene ID | 1494474 |
| Country | Netherland |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | A |
| Sample |
Human |
| 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 | 30708281 |
| Clinical information | Yes |
| Disease | - |
| Published year | 2019 |
| Journal | Journal Of Clinical Virology |
| Title | High epidemic burden of RSV disease coinciding with genetic alterations causing amino acid substitutions in the RSV G-protein during the 2016/2017 season in The Netherlands |
| Author | Laura M Vos, Jan Jelrik Oosterheert, Sacha D Kuil, Marco Viveen, Louis J Bont |
| Evidence | Fig. 3 |