Mutation detail:
Mutation site | L122P |
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 ![]() |
Human |
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 | 2769235 |
Clinical information | No |
Disease | SSPE(Subacute sclerosing panencephalitis) |
Published year | 1989 |
Journal | Journal Of General Virology |
Title | Matrix protein of cell-associated subacute sclerosing panencephalitis viruses |
Author | M Enami ,T A Sato, A Sugiura |
Evidence | Fig.2 |