scholarly journals Tables of Toxicity of Botulinum and Tetanus Neurotoxins

Toxins ◽  
2019 ◽  
Vol 11 (12) ◽  
pp. 686 ◽  
Author(s):  
Ornella Rossetto ◽  
Cesare Montecucco
Keyword(s):  
Biological Activity ◽  
Botulinum Neurotoxin ◽  
Animal Species ◽  
Vesicular Trafficking ◽  
Nerve Terminals ◽  
Molecular Tools ◽  
Botulinum Neurotoxins ◽  
Cholinergic Nerve Terminals ◽  
Metalloprotease Activity ◽  
Internal Comparison

Tetanus and botulinum neurotoxins are the most poisonous substances known, so much so as to be considered for a possible terrorist use. At the same time, botulinum neurotoxin type A1 is successfully used to treat a variety of human syndromes characterized by hyperactive cholinergic nerve terminals. The extreme toxicity of these neurotoxins is due to their neurospecificity and to their metalloprotease activity, which results in the deadly paralysis of tetanus and botulism. Recently, many novel botulinum neurotoxins and some botulinum-like toxins have been discovered. This large number of toxins differs in terms of toxicity and biological activity, providing a potential goldmine for novel therapeutics and for new molecular tools to dissect vesicular trafficking, fusion, and exocytosis. The scattered data on toxicity present in the literature require a systematic organization to be usable by scientists and clinicians. We have assembled here the data available in the literature on the toxicity of these toxins in different animal species. The internal comparison of these data provides insights on the biological activity of these toxins.

Binding of botulinum neurotoxin to pure cholinergic nerve terminals isolated from the electric organ of Torpedo

1992 ◽  
Vol 90 (2) ◽  
pp. 87-102 ◽  
Author(s):  
J. Blasi ◽  
G. Egea ◽  
M. J. Castiella ◽  
M. Arribas ◽  
C. Solsona ◽  
...  
Keyword(s):  
Botulinum Neurotoxin ◽  
Electric Organ ◽  
Nerve Terminals ◽  
Cholinergic Nerve ◽  
Cholinergic Nerve Terminals

scholarly journals Targeted delivery into motor nerve terminals of inhibitors for SNARE-cleaving proteases via liposomes coupled to an atoxic botulinum neurotoxin

FEBS Journal ◽  
2012 ◽  
Vol 279 (14) ◽  
pp. 2555-2567 ◽  
Author(s):  
Om P. Edupuganti ◽  
Saak V. Ovsepian ◽  
Jiafu Wang ◽  
Tomas H. Zurawski ◽  
James J. Schmidt ◽  
...  
Keyword(s):  
Targeted Delivery ◽  
Botulinum Neurotoxin ◽  
Motor Nerve ◽  
Nerve Terminals ◽  
Motor Nerve Terminals

scholarly journals Localization of immunoreactive synthetic atrial natriuretic factor (ANF) in the heart of various animal species.

1985 ◽  
Vol 33 (6) ◽  
pp. 541-550 ◽  
Author(s):  
C Chapeau ◽  
J Gutkowska ◽  
P W Schiller ◽  
R W Milne ◽  
G Thibault ◽  
...  
Keyword(s):  
Biological Activity ◽  
Atrial Natriuretic Factor ◽  
Animal Species ◽  
Rana Catesbeiana ◽  
Protein A ◽  
Antibody Technique ◽  
Natriuretic Factor ◽  
Toad Bufo ◽  
Unlabeled Antibody ◽  
Atrial Natriuretic

The localization of two synthetic fragments of the C-terminal portion of atrial natriuretic factor: Arg 101-Tyr 126 which displays full biological activity and Leu 94-Arg 109 which is completely devoid of biological activity, has been investigated by immunohisto- and immunocytochemical methods in the heart of mammals (rat, mouse, guinea pig, hamster, rabbit, cat, dog, man) and nonmammalian vertebrates toad (Bufo marinus), frog (Rana catesbeiana), fish (Cyprinus carpio, Puntius schwanenfeldi, Cichlosoma biocellatum, Carrasius auratus), snake (Python reticulatus) and hen. Antibodies against the synthetic fragments of ANF were raised in rabbits and used either for immunofluorescence (Coons' technique), immunohistochemistry (unlabeled antibody technique) or immunocytochemistry (protein A-gold technique). Results obtained by immunofluorescence and by the unlabeled antibody technique were similar: antibodies against Arg 101-Tyr 126 ANF allowed visualization of granulated cardiocytes in the atria of all mammals. While the reaction was very strong in rat and mouse, it was less so in the rabbit and very weak in all other species studied including man. Antibodies against Leu 94-Arg 109 ANF produced a reaction only in the rat and mouse. In nonmammalian vertebrates, the reaction was always much stronger in atria than ventricles of all species with both antibodies.

Nicotinamide adenine dinucleotide is released from sympathetic nerve terminals via a botulinum neurotoxin A-mediated mechanism in canine mesenteric artery

2006 ◽  
Vol 290 (5) ◽  
pp. H1818-H1825 ◽  
Author(s):  
Lisa M. Smyth ◽  
Leanne T. Breen ◽  
Violeta N. Mutafova-Yambolieva
Keyword(s):  
Neural Activity ◽  
Nicotinamide Adenine Dinucleotide ◽  
High Performance ◽  
Botulinum Neurotoxin ◽  
Mesenteric Arteries ◽  
Nicotinamide Adenine ◽  
System Control ◽  
Nerve Terminals ◽  
Botulinum Neurotoxin A ◽  
Different Populations

Using high-performance liquid chromatography techniques with fluorescence and electrochemical detection, we found that β-nicotinamide adenine dinucleotide (β-NAD) is released in response to electrical field stimulation (4–16 Hz, 0.3 ms, 15 V, 120 s) along with ATP and norepinephrine (NE) in the canine isolated mesenteric arteries. The release of β-NAD increases with number of pulses/stimulation frequencies. Immunohistochemistry analysis showed dense distribution of tyrosine hydroxylase-like immunoreactivity (TH-LI) and sparse distribution of TH-LI-negative nerve processes, suggesting that these blood vessels are primarily under sympathetic nervous system control with some contribution of other (e.g., sensory) neurons. Exogenous NE (3 μmol/l), α,β-methylene ATP (1 μmol/l), neuropeptide Y (NPY, 0.1 μmol/l), CGRP (0.1 μmol/l), vasoactive intestinal peptide (VIP, 0.1 μmol/l), and substance P (SP, 0.1 μmol/l) had no effect on the basal release of β-NAD, suggesting that the overflow of β-NAD is evoked by neither the sympathetic neurotransmitters NE, ATP, and NPY, nor the neuropeptides CGRP, VIP, and SP. Botulinum neurotoxin A (BoNTA, 0.1 μmol/l) abolished the evoked release of NE, ATP, and β-NAD at 4 Hz, suggesting that at low levels of neural activity, release of these neurotransmitters results from N-ethylmaleimide-sensitive factor attachment protein receptor/synaptosomal-associated protein of 25 kDa-mediated exocytosis. At 16 Hz, however, the evoked release of NE, ATP, and β-NAD was reduced by BoNTA by ∼90, 60, and 80%, respectively, suggesting that at higher levels of neural activity, β-NAD is likely to be released from different populations of synaptic vesicles or different populations of nerve terminals (i.e., sympathetic and sensory terminals).

scholarly journals Variations in the Botulinum Neurotoxin Binding Domain and the Potential for Novel Therapeutics

Toxins ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 421 ◽  
Author(s):  
Jonathan Davies ◽  
Sai Liu ◽  
K. Acharya
Keyword(s):  
Botulinum Neurotoxin ◽  
Neuronal Cell ◽  
Binding Domain ◽  
Novel Therapeutics ◽  
Specific Targeting ◽  
Zinc Metalloprotease ◽  
Botulinum Neurotoxins ◽  
Translocation Domain ◽  
Subtype Differences

Botulinum neurotoxins (BoNTs) are categorised into immunologically distinct serotypes BoNT/A to /G). Each serotype can also be further divided into subtypes based on differences in amino acid sequence. BoNTs are ~150 kDa proteins comprised of three major functional domains: an N-terminal zinc metalloprotease light chain (LC), a translocation domain (HN), and a binding domain (HC). The HC is responsible for targeting the BoNT to the neuronal cell membrane, and each serotype has evolved to bind via different mechanisms to different target receptors. Most structural characterisations to date have focussed on the first identified subtype within each serotype (e.g., BoNT/A1). Subtype differences within BoNT serotypes can affect intoxication, displaying different botulism symptoms in vivo, and less emphasis has been placed on investigating these variants. This review outlines the receptors for each BoNT serotype and describes the basis for the highly specific targeting of neuronal cell membranes. Understanding receptor binding is of vital importance, not only for the generation of novel therapeutics but also for understanding how best to protect from intoxication.

scholarly journals Botulism (type A) in a horse - case report

2016 ◽  
Vol 85 (1) ◽  
pp. 71-76 ◽  
Author(s):  
Sevim Kasap ◽  
Hasan Batmaz ◽  
Meric Kocaturk ◽  
Frank Gessler ◽  
Serkan Catık ◽  
...  
Keyword(s):  
Botulinum Neurotoxin ◽  
Clinical Signs ◽  
Type A ◽  
Serum Samples ◽  
Specific Antibodies ◽  
Thoroughbred Horse ◽  
Botulinum Neurotoxin Type A ◽  
Botulinum Neurotoxins ◽  
First Time ◽  
Colonic Content

This paper presents the case of a six year-old, male, thoroughbred horse with clinical signs of inappetence, weakness, and incoordination when walking. Clinical examination showed that the horse staggered and leaned to the left side. Feedstuff was present inside and around its mouth. Salivation was increased and there was no reflex at the palpebrae and tongue. The horse had difficulty swallowing and the tone of its tail was reduced. Botulism was diagnosed based on the clinical signs. Antibiotic (ceftiofur) and fluid-electrolyte treatment was commenced. Next day, neostigmin was added to the horse’s treatment, and it became recumbent. The horse’s palpebral, tongue and tail reflexes returned partially after neostigmine methylsulphate treatment on the same day and it stood up on day four. However, it could not swallow anything during the whole week, so after getting permission from the owner, the horse was euthanized on day 10. Samples of the colonic content and blood serum were sent by courier to the laboratory for toxin neutralization, however, botulinum neurotoxins could not be detected. After that, serum samples from days 6 and 10 were sent to another laboratory for testing for botulinum neurotoxin antibodies by ELISA. Specific antibodies against botulinum neurotoxin type A were measured, indicating a previous, immuno-relevant contact with the toxin. This seroconversion for type A supports the clinical botulism diagnosis. Type A botulism is rarely seen in Europe and has been detected in a horse in Turkey for the first time.

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