| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/907 |
| landingPage: |
http://www.iedb.org/assay/10496 |
| type: |
Literature
|
| publicationVenue: |
Virology
|
| dates: |
2002
|
| study type: | b cell assays |
| subject species: | Influenza A virus (A/tern/Australia/G70C/1975(H11N9)) |
| fullName: |
Janis T Lee
Gillian M Air
|
| method: |
ELISA
|
| name: |
Contacts between influenza virus N9 neuraminidase and monoclonal antibody NC10.
|
| description: |
The epitope residues positions used in the paper are those relative to the N2 sequence to allow easy comparison with the structure. Mutagenesis in this work was based on crystal structure of the complex between N9 and Fab NC10 and data from viral escape mutants. Overall 7 NA mutants were generated, four at residues forming H-bonds (N327Q, S371T, S373A, N400L), one that forms a salt bridge with the Fab (K434M), and one that removes the N-linked oligosaccharide which forms part of the epitope (N200L).
Kd (apparent) and Kcat was compared to wild-type binding and catalytic rate constants. N200L mutant had a significantly reduced (~80%) Kcat and reduced binding affinity thought to be due to a defect in assembly or folding. Other mutants had similar Kcat values and binding affinities, indicating the contacting amino acids on the Ab could accommodate all mutations.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |