Mutation detail:
| Mutation site | R293Q |
| 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 | AB016162.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
increase |
| 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 | 33916225 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Viruses |
| Title | Mutated Measles Virus Matrix and Fusion Protein Influence Viral Titer In Vitro and Neuro-Invasion in Lewis Rat Brain Slice Cultures |
| Author | Johannes Busch,Soroth Chey,Michael Sieg,Thomas W Vahlenkamp,Uwe G Liebert |
| Evidence | A mutation in the carboxy-terminal domain of the matrix protein (R293Q) promoted the production of progeny virions. This effect was observed in Vero cells irrespective of the expression of the signaling lymphocyte activation molecule (SLAM). Furthermore, |