Molecular immune recognition of botulinum neurotoxin B. The light chain regions that bind human blocking antibodies from toxin-treated cervical dystonia patients. Antigenic structure of the entire BoNT/B molecule

Enhancing the Protective Immune Response against Botulism

“…Previously, our lab engineered a vaccine composed of the HCR domains of each of the seven BoNT serotypes which protected against challenge by each respective holotoxin (33). A lack of cross-neutralization is consistent with the observation that immunoreactive epitopes appear to be distinct for different serotypes, as reported for BoNT/A and BoNT/B (30,34).…”

Botulinum Neurotoxins: Biology, Pharmacology, and Toxicology

“…Antibodies formed against the accessory proteins do not interfere with the biologic activity of the toxin, and they are therefore nonneutralizing antibodies, whereas antibodies formed against the neurotoxin (primarily against the heavy chain) may prevent or not prevent its biologic activity. Those antibodies that prevent it are neutralizing antibodies and are expected to interfere with the clinical efficacy of the product (Dolimbek et al, 2007; Atassi et al, 2012). However, all BoNT serotypes can be considered poor antigens, particularly with respect to the cousin molecule tetanus neurotoxin.…”

Molecular basis of immunogenicity to botulinum neurotoxins and uses of the defined antigenic regions

“…The BoNT/A regions recognized by human Abs were mapped with synthetic 19-residue peptides that overlapped by 5 residues and covered the entire BoNT/A and BoNT/B molecules The epitopes were mapped with anti-Toxin Abs of mouse, horse, chicken and human (Atassi et al, 1996(Atassi et al, , 2012aAtassi and Dolimbek, 2004;Dolimbek et al, 2008, Dolimbek et al, 2011a. Blocking (protective) Abs from 28 CD patients who had mounted immune resistance to treatment with BoNT/A were also used .…”