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identifier: 1809066
description:
epitope description:YTTSTRGDLAHVTAT
antigen name:Polyprotein
host organism:Mus musculus BALB/c
antibody name:3E5
aggregation:
instance of dataset
availability:
available
primaryPublications: 11395136
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.

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