Mutation detail:
| Mutation site | P64S |
| Virus | Measles virus |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | M |
| Gene ID | 1489803 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | K01711.1 |
| 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 | P35976 |
| Protein length | 335 amino acids |
| Protein description | The M protein is thought to drive MeV assembly by physically recruiting the RNP and glycoproteins to the host cell plasma membrane. Studies have shown that altered interaction between M and the cytoplasmic tail of H or F affects MeV viral growth, indicating the necessity for contacts between M and the glycoproteins during assembly. Recent structural studies of NDV by cryo-ET and X-ray crystallography demonstrated that the RNP complex is aligned with M protein arrays16. Furthermore, it has been suggested that actin filaments play a role in the MeV assembly and budding process by facilitating the transportation of M-RNP complexes. |
Literature information:
| Pubmed ID | 17442724 |
| Clinical information | No |
| Disease | - |
| Published year | 2007 |
| Journal | Journal of Virology |
| Title | Altered interaction of the matrix protein with the cytoplasmic tail of hemagglutinin modulates measles virus growth by affecting virus assembly and cell-cell fusion |
| Author | Maino Tahara,Makoto Takeda,Yusuke Yanagi |
| Evidence | When the cytoplasmic tail of the H protein is deleted, a virus with an M protein possessing the P64S and E89K substitutions no longer grows well in Vero cells yet causes cell-cell fusion and replicates efficiently in B95a cells. |