Mutation detail:
| Mutation site | M53V |
| Virus | Measles virus |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | M |
| Gene ID | 1489803 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | B3 |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | EF565857.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | Yes |
| 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 | 24648840 |
| Clinical information | No |
| Disease | - |
| Published year | 2014 |
| Journal | Archives of Virology |
| Title | Mutations in the H, F, or M Proteins Can Facilitate Resistance of Measles Virus to Neutralizing Human Anti-MV Sera |
| Author | Hasan Kweder , Michelle Ainouze , Sara Louise Cosby , Claude P Muller , Camille Levy |
| Evidence | Table1 |