Mutation detail:
| Mutation site | K272N |
| 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 | AY911262.1/M11486.1 |
| Drug/antibody/vaccine | Palivizumab-resistant |
| 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 | 21208913 |
| Clinical information | No |
| Disease | - |
| Published year | 2011 |
| Journal | The Journal of infectious diseases |
| Title | Analysis of Respiratory Syncytial Virus Preclinical and Clinical Variants Resistant to Neutralization by Monoclonal Antibodies Palivizumab and/or Motavizumab |
| Author | Qing Zhu,Josie M. McAuliffe,Nita K. Patel,Frances J. Palmer-Hill,Chin-fen Yang |
| Evidence | The palivizumab-selected clones B1, B2, B7, and B9 containing mutations K272N, K272M, K272T, or K272Q were largely resistant to palivizumab neutralization, with increases in calculated IC50 values ranging from 5164-fold for clone B1 to >25,000-fold for B2 |