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Botulinum neurotoxins (BoNTs) are the most toxic substances known. BoNT intoxicates cells in a highly programmed fashion initiated by binding to the cell surface, internalization and enzymatic cleavage of substrate, thus, inhibiting synaptic exocytosis. Over the past two decades, immunological significance of BoNT/A C-terminal heavy chain (H C ) and light chain (L C ) domains were investigated extensively leading to important findings. In the current work, we explored the significance of BoNT/A heavy chain N-terminal (H N ) region as a vaccine candidate. Mice were immunized with recombinant H N 519–845 generating antibodies (Abs) that were found to be protective against lethal dose of BoNT/A. Immuno-dominant regions of H N 519–845 were identified and individually investigated for antibody response along with synthetic peptides within those regions, using  in vivo  protection assays against BoNT/A. Results were confirmed by patch-clamp analysis where anti-H N  antibodies were studied for the ability to block toxin-induced channel formation. This data strongly indicated that H N 519–593 is an important region in generating protective antibodies and should be valuable in a vaccine design. These results are the first to describe and dissect the protective activity of the BoNT/A H N  domain.

Antigenic sites on the HN domain of botulinum neurotoxin A stimulate protective antibody responses against active toxin