| identifier: | 1275968 |
| description: |
epitope description:G145, V146, T147, Q148, N149, G150, G151, S152, N153, T171, K172, S173, G174, S175, E206, S209, L210
antigen name:Hemagglutinin
host organism:Mus musculus BALB/c
antibody name:HC19
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
9461077 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1100 |
| landingPage: |
http://www.iedb.org/assay/1275968 |
| type: |
Literature
|
| publicationVenue: |
Nat Struct Biol
|
| dates: |
1998
|
| study type: | b cell assays |
| subject species: | Influenza A virus (A/X-31(H3N2)) |
| fullName: |
D Fleury
S A Wharton
J J Skehel
M Knossow
T Bizebard
|
| method: |
ELISA
|
| name: |
Antigen distortion allows influenza virus to escape neutralization.
|
| description: |
The epitope residues were calculated from the WT antigen-antibody complex structure [PDB: 2VIR] as the antigen residues at 4Å
atomic distance from the antibody. In [PDB: 2VIS], the antigen is mutated such that contact residue T131 is changed to I131. In [PDB: 2VIT], the antigen is mutated such that contact residue T155 is changed to I155 and an additional contact residue W153 is observed.
The binding of epitope-specific HC19 Fab to the wild type and mutant HAs was measured. The Fab bound the T131l and S157L mutant HAs with a 4000-fold and 500-fold reduced affinity, respectively, compared to that of Fab to wild-type HA.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |