Alanine-scanning mutations in domain 4 of anthrax toxin protective antigen reveal residues important for binding to the cellular receptor and to a neutralizing monoclonal antibody.

Title:

Alanine-scanning mutations in domain 4 of anthrax toxin protective antigen reveal residues important for binding to the cellular receptor and to a neutralizing monoclonal antibody.

Dataset

identifier:	1369941
description:	epitope description:N711, K713, L714, P715, L716, Y717 antigen name:Protective antigen host organism:Mus musculus BALB/c antibody name:14B7
aggregation:	instance of dataset
availability:	available
primaryPublications:	12771151

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1003646
landingPage:	http://www.iedb.org/assay/1369941

Publication

type:	Literature
publicationVenue:	J Biol Chem
dates:	2003

Dimension

study type:	b cell assays
subject species:	Bacillus anthracis

Person

fullName:	M J Rosovitz Peter Schuck Mini Varughese Arun P Chopra Varsha Mehra Yogendra Singh Lisa M McGinnis Stephen H Leppla

Data Type

method:	surface plasmon resonance (SPR)

Study

name:	Alanine-scanning mutations in domain 4 of anthrax toxin protective antigen reveal residues important for binding to the cellular receptor and to a neutralizing monoclonal antibody.
description:	These residues are located at the small loop of domain 4 of PA, a region that had been involved in the recognition by neutralizing antibodies. The neutralizing mAb 14B7 was analyzed in its affinity to WT PA and alanine mutants to study the contribution of individual residues to binding. The residues listed were detrimental to the binding affinity by factors ranging from >10,000- to 18-fold. Affinity was also analyzed by sedimentation equilibrium , with similar results (KD <6nM for WT PA).

Data Repository

name:	iedb
homePage:	http://www.iedb.org

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