Mutation detail:
Mutation site | I98T |
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 | 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 | 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 | 17626104 |
Clinical information | No |
Disease | - |
Published year | 2007 |
Journal | Journal of Virology |
Title | Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein |
Author | Elizabeth A Corey,Ronald M Iorio |
Evidence | The roles of the heptadic residues (I84, V91, I98, and L105) in the fusion process were examined by the introduction of an alanine substitution at each of these positions in the MV H protein and by characterization of the mutated proteins. |