Nerve terminals are specific sites of action of a very large number of toxins produced by many different organisms. The mechanism of action of three groups of presynaptic neurotoxins that interfere directly with the process of neurotransmitter release is reviewed, whereas presynaptic neurotoxins acting on ion channels are not dealt with here. These neurotoxins can be grouped in three large families: 1) the clostridial neurotoxins that act inside nerves and block neurotransmitter release via their metalloproteolytic activity directed specifically on SNARE proteins; 2) the snake presynaptic neurotoxins with phospholipase A(2) activity, whose site of action is still undefined and which induce the release of acethylcholine followed by impairment of synaptic functions; and 3) the excitatory latrotoxin-like neurotoxins that induce a massive release of neurotransmitter at peripheral and central synapses. Their modes of binding, sites of action, and biochemical activities are discussed in relation to the symptoms of the diseases they cause. The use of these toxins in cell biology and neuroscience is considered as well as the therapeutic utilization of the botulinum neurotoxins in human diseases characterized by hyperfunction of cholinergic terminals.

https://www.physiology.org/doi/pdf/10.1152/physrev.2000.80.2.717

Neurotoxins Affecting Neuroexocytosis

α-Latrotoxin: from structure to some functions

For more than three decades, the venom of the black widow spider and its principal active components, latrotoxins, have been used to induce release of neurotransmitters and hormones and to study the mechanisms of exocytosis. Given the complex nature of α-latrotoxin actions, this research has been continuously overshadowed by many enigmas, misconceptions and perpetual changes of the underlying hypotheses. Some of the toxin’s mechanisms of action are still not completely understood. Despite all these difficulties, the extensive work of several generations of neurobiologists has brought about a great deal of fascinating insights into presynaptic processes and has led to the discovery of several novel proteins and synaptic systems. For example, α-latrotoxin studies have contributed to the widespread acceptance of the vesicular theory of transmitter release. Presynaptic receptors for α-latrotoxin – neurexins, latrophilins and protein tyrosine phosphatase σ – and their endogenous ligands have now become centerpieces of their own areas of research, with a potential of uncovering new mechanisms of synapse formation and regulation that may have medical implications. However, any future success of α-latrotoxin research will require a better understanding of this unusual natural tool and a more precise dissection of its multiple mechanisms.

Penelope’s web: using α‐latrotoxin to untangle the mysteries of exocytosis

Mechanism of α-latrotoxin action as revealed by patch-clamp experiments onXenopus oocytes injected with rat brain messenger RNA

Vitamin B1 thiazole derivative reduces transmembrane current through ionic channels formed by toxins from black widow spider venom and sea anemone in planar phospholipid membranes.

Highly purified protein preparations promoting TTX-dependent sodium permeability in the liposomal membrane were separated from the cytoplasmic fraction of bovine brain tissue. The protein was purified using anion-exchange and separation chromatography and gel filtration. The separated protein was found to be a high-molecular acidic glycoprotein forming 55 kD subunits during denaturation under reducing conditions. It was thought to contribute to the formation of voltage-dependent sodium channels in the cell membrane.

Purification of soluble tetrodotoxin-sensitive protein from the cytoplasmic fraction of bovine brain tissue

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2892%2980849-C

Latrotoxin‐like properties of a protein from brain

Interaction of tetrodotoxin-sensitive proteins of the soluble cytoplasmic fraction of mammalian brain with liposomes was studied. Tetrodotoxin-sensitive proteins were shown to be incorporated in an orderly transmembrane manner into liposomes of a particular chemical composition (phosphatidylcholine-phosphatidylserine-cholesterol, brain phospholipids-cholesterol).

Integration of soluble tetrodotoxin-sensitive brain proteins with liposomal membranes

Probing the structure-function relationship of α-latrotoxin-formed channels with antibodies and pronase

The peculiarities of interaction of TTX-sensitive soluble cytoplasmic brain fraction proteins with liposomes were studied. It was shown that transmembrane orientated insertion of TTX-sensitive proteins into liposomes depends on chemical composition of their lipids.

[Integration of soluble tetrodotoxin-sensitive brain proteins into membrane liposomes].

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