Mutation detail:
| Mutation site | T205A |
| Virus | Human respiratory syncytial virus |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | M |
| Gene ID | 1494472 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | A |
| 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 | Matrix Protein |
| Uniprot protein ID | P0DOE7 |
| Protein length | 256 amino acids |
| Protein description | Matrix Protein, a non-glycosylated inner virion protein, plays a central role in infection. It is smaller than its paramyxovirus counterparts (256 a.a as compared to 335-375 a.a) and shares no clear sequence homology with them. All paramyxovirus M proteins are known to be strongly membrane-associated and have similar hydropathy profiles. There is a common region of low hydrophobicity at the N-terminus followed by a gradual increase in hydrophobic value towards the C-terminus, which includes a highly hydrophobic region. The hydrophobic regions are smaller than the minimum required for a transmembrane domain, but may mediate peripheral attachment to the host cell membrane. |
Literature information:
| Pubmed ID | 24672034 |
| Clinical information | No |
| Disease | - |
| Published year | 2014 |
| Journal | Journal of virology |
| Title | The Thr205 Phosphorylation Site within Respiratory Syncytial Virus Matrix (M) Protein Modulates M Oligomerization and Virus Production |
| Author | M.Bajorek,L.Caly,K.C.Tran,G.N.Maertens,R.A.Tripp |
| Evidence | To test for the importance of Thr205 in RSV infection, we substituted Thr205 to either a nonphosphorylatable Ala (T205A) or phosphomimetic Asp (T205D) residue in the context of the full-length RSV A2 antigenome using reverse genetics (40). Although RSV wi |