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Review
, 11 (9)

Antibodies and Vaccines Against Botulinum Toxins: Available Measures and Novel Approaches

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Review

Antibodies and Vaccines Against Botulinum Toxins: Available Measures and Novel Approaches

Christine Rasetti-Escargueil et al. Toxins (Basel).

Abstract

Botulinum neurotoxin (BoNT) is produced by the anaerobic, Gram-positive bacterium Clostridium botulinum. As one of the most poisonous toxins known and a potential bioterrosism agent, BoNT is characterized by a complex mode of action comprising: internalization, translocation and proteolytic cleavage of a substrate, which inhibits synaptic exocytotic transmitter release at neuro-muscular nerve endings leading to peripheral neuroparalysis of the skeletal and autonomic nervous systems. There are seven major serologically distinct toxinotypes (A-G) of BoNT which act on different substrates. Human botulism is generally caused by BoNT/A, B and E. Due to its extreme lethality and potential use as biological weapon, botulism remains a global public health concern. Vaccination against BoNT, although an effective strategy, remains undesirable due to the growing expectation around therapeutic use of BoNTs in various pathological conditions. This review focuses on the current approaches for botulism control by immunotherapy, highlighting the future challenges while the molecular underpinnings among subtypes variants and BoNT sequences found in non-clostridial species remain to be elucidated.

Keywords: BoNT variants; antibodies; antitoxin; botulinum neurotoxins (BoNTs); vaccines.

Conflict of interest statement

The authors declare no conflict of interest. They were previously involved in AntiBotABE program but with no present financial interest.

Figures

Figure 1
Figure 1
Epitope mapping of neutralizing antibodies (red); Blue: light chain (LC), pink: H chain (HN), yellow: HC N-terminal moiety (HCn) and HC C-terminal moiety (HCc).
Figure 1
Figure 1
Epitope mapping of neutralizing antibodies (red); Blue: light chain (LC), pink: H chain (HN), yellow: HC N-terminal moiety (HCn) and HC C-terminal moiety (HCc).

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