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Volume 11, Number 10—October 2005

Research

Botulinum Neurotoxin Detection and Differentiation by Mass Spectrometry

John R. Barr*Comments to Author , Hercules Moura*, Anne E. Boyer*, Adrian R. Woolfitt*, Suzanne R. Kalb*, Antonis Pavlopoulos*, Lisa G. McWilliams†, Jurgen G. Schmidt‡, Rodolfo A. Martinez‡, and David L. Ashley*
Author affiliations: *Centers for Disease Control and Prevention, Atlanta, Georgia, USA; †Battelle Memorial Institute, Atlanta, Georgia, USA; ‡Los Alamos National Laboratory, Los Alamos, New Mexico, USA

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Figure 1

Synaptobrevin on the synaptic vesicle must interact with syntaxin and SNAP (synaptosomal-associated protein)-25 on the neuronal membrane for fusion to occur, which allows the nerve impulse to be delivered across the synaptic junction. The botulinum neurotoxin serotypes cleave the peptide bonds at specific sites on the 3 proteins, as indicated. Cleavage of any 1 of these proteins prevents vesicle membrane docking and nerve impulse transmission.

Figure 1. Synaptobrevin on the synaptic vesicle must interact with syntaxin and SNAP (synaptosomal-associated protein)-25 on the neuronal membrane for fusion to occur, which allows the nerve impulse to be delivered across the synaptic junction. The botulinum neurotoxin serotypes cleave the peptide bonds at specific sites on the 3 proteins, as indicated. Cleavage of any 1 of these proteins prevents vesicle membrane docking and nerve impulse transmission.

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