Production and characterization of neutralizing monoclonal antibodies that recognize an epitope in domain 2 of Bacillus anthracis protective antigen.
Antibodies against the protective antigen (PA) of Bacillus anthracis play a key role in response to infection by this important pathogen. The aim of this study was to produce and characterize monoclonal antibodies (mAbs) specific for PA and to identify novel neutralizing epitopes. Three murine mAbs with high specificity and nanomolar affinity for B. anthracis recombinant protective antigen (rPA) were produced and characterized. Western immunoblot analysis, coupled with epitope mapping using overlapping synthetic peptides, revealed that these mAbs recognize a linear epitope within domain 2 of rPA. Neutralization assays demonstrate that these mAbs effectively neutralize lethal toxin in vitro.
Gubbins
Michael J
MJ
Division of Vaccine Preventable Diseases, National Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, MB, Canada.
Berry
Jody D
JD
Corbett
Cindi R
CR
Mogridge
Jeremy
J
Yuan
Xin Y
XY
Schmidt
Lisa
L
Nicolas
Brigitte
B
Kabani
Amin
A
Tsang
Raymond S
RS
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis / Q000276:immunology*; D000942:Antigens, Bacterial / Q000276:immunology*; D001408:Bacillus anthracis / Q000276:immunology*; D001427:Bacterial Toxins / Q000276:immunology*; D001666:Binding Sites, Antibody; D018604:Epitope Mapping; D000939:Epitopes; D051379:Mice; D008807:Mice, Inbred BALB C; D009500:Neutralization Tests; D017434:Protein Structure, Tertiary
D000911:Antibodies, Monoclonal; D000942:Antigens, Bacterial; D001427:Bacterial Toxins; D000939:Epitopes; C030325:anthrax toxin