Mutation detail:
Mutation site | N465H |
Virus | Measles virus |
Mutation level ![]() |
Amino acid Level |
Gene/protein/region type | F |
Gene ID | 1489800 |
Country | Japan |
Mutation type ![]() |
nonsynonymous mutation |
Genotype/subtype/clade | H1 |
Sample ![]() |
cell line |
Variants | - |
Viral reference sequence | AB968383.1 |
Drug/antibody/vaccine | - |
Transmissibility ![]() |
- |
Transmission mechanism | - |
Pathogenicity ![]() |
- |
Pathogenicity mechanism | - |
Immune escape mutation | - |
Immune escape mechanism | - |
RT-PCR primers probes | - |
Protein detail:
Protein name | Fusion Protein |
Uniprot protein ID | P69358 |
Protein length | 550 amino acids |
Protein description | Fusion Protein is class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. |
Literature information:
Pubmed ID | 25479085 |
Clinical information | No |
Disease | - |
Published year | 2015 |
Journal | FEBS Letters |
Title | Intramolecular complementation of measles virus fusion protein stability confers cell-cell fusion activity at 37C |
Author | Yuto Satoh,Mitsuhiro Hirose,Hiroko Shogaki,Hiroshi Wakimoto,Yoshinori Kitagawa |
Evidence | The N465H substitution in the heptad repeat B domain of the stalk region of the F protein eliminates this activity, but an additional mutation in the DIII domain of the head region - N183D, F217L, P219S, I225T or G240R - restores cell-cell fusion. |