AVM v1, released 02-OCT-22

A manually curated database of aerosol-transmitted virus mutations, human diseases, and drugs

Mutation detail:


Mutation site V101A
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 17217427
Clinical information No
Disease SSPE(Subacute sclerosing panencephalitis)
Published year 2007
Journal Cellular Microbiology
Title Measles virus nucleocapsid transport to the plasma membrane requires stable expression and surface accumulation of the viral matrix protein
Author Nicole Runkler,Christine Pohl,Sibylle Schneider-Schaulies,Hans-Dieter Klenk,Andrea Maisner
Evidence Although MV101A was rapidly degraded in infected cells, the turnover of MV101A was slower than in cells transfected to express M protein alone suggesting that virus infection either slows down the degradation machinery or MV101A is stabilized by other vir