Mutation detail:
Mutation site | N481Y/H495R |
Virus | Measles virus |
Mutation level ![]() |
Amino acid Level |
Gene/protein/region type | H |
Gene ID | 1489801 |
Country | - |
Mutation type ![]() |
nonsynonymous mutation |
Genotype/subtype/clade | - |
Sample ![]() |
cell line |
Variants | - |
Viral reference sequence | AB016162.1 |
Drug/antibody/vaccine | - |
Transmissibility ![]() |
- |
Transmission mechanism | - |
Pathogenicity ![]() |
- |
Pathogenicity mechanism | - |
Immune escape mutation | - |
Immune escape mechanism | - |
RT-PCR primers probes | - |
Protein detail:
Protein name | Hemagglutinin Protein |
Uniprot protein ID | P08362 |
Protein length | 617 amino acids |
Protein description | Hemagglutinin Protein attaches the virus to cell receptors and thereby initiating infection. Binding of H protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion. May use human CD46 and/or SLAMF1 as receptors for viral entry into the cell. The high degree of interaction between H and MCP/CD46 results in down-regulation of the latter from the surface of infected cells, rendering them more sensitive to c3b-mediated complement lysis. |
Literature information:
Pubmed ID | 19553316 |
Clinical information | No |
Disease | - |
Published year | 2009 |
Journal | Journal of Virology |
Title | Previously unrecognized amino acid substitutions in the hemagglutinin and fusion proteins of measles virus modulate cell-cell fusion, hemadsorption, virus growth, and penetration rate |
Author | Hiromi Okada,Masae Itoh,Kyosuke Nagata,Kaoru Takeuchi |
Evidence | Interestingly, a recombinant wild-type MV strain harboring the H(N481Y/H495R) protein penetrated slowly into Vero cells, while a recombinant wild-type MV strain harboring both the F(D439E/G464W) and H(N481Y/H495R) proteins penetrated efficiently into Vero |