Abstract
This study describes the isolation and characterization of a neutralizing monoclonal antibody (mAb) against anthrax edema factor, EF13D. EF13D neutralized edema toxin (ET)-mediated cyclic AMP (cAMP) responses in cells and protected mice from both ET-induced footpad edema and systemic ET-mediated lethality. The antibody epitope was mapped to domain IV of EF. The mAb was able to compete with calmodulin (CaM) for EF binding and displaced CaM from EF-CaM complexes. EF-mAb binding affinity (0.05-0.12 nM) was 50- to 130-fold higher than that reported for EF-CaM. This anti-EF neutralizing mAb could potentially be used alone or with an anti-PA mAb in the emergency prophylaxis and treatment of anthrax infection.
Publication types
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Research Support, N.I.H., Intramural
MeSH terms
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Animals
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Antibodies, Monoclonal / immunology*
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Antibodies, Monoclonal / isolation & purification
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Antibody Affinity
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Antigens, Bacterial / chemistry
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Antigens, Bacterial / immunology*
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Bacterial Toxins / chemistry
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Bacterial Toxins / immunology*
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Binding, Competitive*
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Calmodulin / metabolism*
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Edema / chemically induced
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Edema / immunology
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Edema / prevention & control
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Humans
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Immunoglobulin Fab Fragments / immunology
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Mice
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Neutralization Tests
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Pan troglodytes / immunology
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Protein Binding
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Protein Structure, Tertiary
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Ultracentrifugation
Substances
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Antibodies, Monoclonal
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Antigens, Bacterial
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Bacterial Toxins
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Calmodulin
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Immunoglobulin Fab Fragments
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anthrax toxin