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Infection and Immunity, January 2001, p. 570-574, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.570-574.2001

High-Affinity, Protective Antibodies to the Binding Domain of Botulinum Neurotoxin Type A

Dorothy D. Pless, Edna R. Torres, Emily K. Reinke, and Sina Bavari^*

Department of Cell Biology and Biochemistry, U.S. Army Medical Research Institute of Infectious Diseases, Frederick, Maryland 21702-5011

Received 7 July 2000/Returned for modification 31 August 2000/Accepted 3 October 2000

Monoclonal antibodies (MAbs) were prepared against the putative binding domain of botulinum neurotoxin A (BoNT/A), a nontoxic 50-kDa fragment. Initially, all fusion products were screened against the holotoxin BoNT/A and against the binding fragment, BoNT/A H_C. Eleven neutralizing hybridomas were cloned, and their specific binding to BoNT/A H_C was demonstrated by surface plasmon resonance, with dissociation constants ranging from 0.9 to <0.06 nM. Epitope mapping by real-time surface plasmon resonance showed that the antibodies bound to at least two distinct regions of the BoNT/A H_C fragment. These MAbs will be useful tools for studying BoNT/A interactions with its receptor, and they have potential diagnostic and therapeutic applications.

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^* Corresponding author. Mailing address: Department of Cell Biology and Biochemistry, U.S. Army Medical Research Institute of Infectious Diseases, 1425 Porter St., Frederick, MD 21702-5011. Phone: (301) 619-4246. Fax: (301) 619-2348. E-mail: Sina.Bavari{at}AMEDD.Army.Mil.

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Infection and Immunity, January 2001, p. 570-574, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.570-574.2001

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