| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1008393 |
| landingPage: |
http://www.iedb.org/assay/1809066 |
| type: |
Literature
|
| publicationVenue: |
Mol Immunol
|
| dates: |
2000
|
| study type: | b cell assays |
| subject species: | Foot-and-mouth disease virus C1 CS30 |
| fullName: |
P Gomes
E Giralt
D Andreu
|
| method: |
surface plasmon resonance (SPR)
|
| name: |
Molecular analysis of peptides from the GH loop of foot-and-mouth disease virus C-S30 using surface plasmon resonance: a role for kinetic rate constants.
|
| description: |
The VP1 sequence for this isolate could not be found in the current GenBank database. An internal identifier is therefore provided.
The affinity of the mAb for the epitope, which has amino acid substitutions A3T and L12V compared to the homologous sequence in the eliciting strain, was measured. The affinity of the mAb for peptides mutated at four positions involved in inter-strain variation showed that substitution L12V, and to a lesser extent A3T, reduced binding significantly by increasing the rate of dissociation. MAb 3E5 did not interact with the triple mutant with residues 138T, 140T, 147V. SPR analysis with immobilized peptide and mAb in the soluble phase gave similar binding kinetics.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |