The toxin Tx4(6-1) from the spider Phoneutria nigriventer slows down Na+ current inactivation in insect CNS via binding to receptor site 3

Lima, Maria Elena de; Stankiewicz, Maria; Hamon, Alain; Figueiredo, Suely G.; Cordeiro, Marta N.; Diniz, Carlos R.; Martin‐Eauclaire, Marie‐France; Pelhate, M.

doi:10.1016/s0022-1910(01)00143-3

Cited by 54 publications

(34 citation statements)

References 38 publications

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“…Moreover, a similar effect is characteristic of some spider toxins binding to site 3 (16,17) and, what is worthy of note, site 4 (18). Promotion of sodium channel activation is also quite widespread among toxins: scorpion ␤-toxins (19) and some spider toxins (20) binding to site 4 show this kind of effect.…”

mentioning

confidence: 75%

Structure of Membrane-active Toxin from Crab Spider Heriaeus melloteei Suggests Parallel Evolution of Sodium Channel Gating Modifiers in Araneomorphae and Mygalomorphae

Berkut

Peigneur

Myshkin

et al. 2015

Journal of Biological Chemistry

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Background: Several toxins from mygalomorph spiders are known to inhibit sodium channel activation. Results: Hm-3 toxin from the araneomorph spider Heriaeus melloteei inhibits mammalian and insect sodium channel activation and possesses membrane activity. Conclusion: Hm-3 binds to sodium channel voltage sensors through membrane access. Significance: The first sodium channel activation inhibitor from Araneomorphae points to parallel evolution of H. melloteei and its distant mygalomorph relatives.

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mentioning

confidence: 75%

Structure of Membrane-active Toxin from Crab Spider Heriaeus melloteei Suggests Parallel Evolution of Sodium Channel Gating Modifiers in Araneomorphae and Mygalomorphae

Berkut

Peigneur

Myshkin

et al. 2015

Journal of Biological Chemistry

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“…The effects of Tx4(6-1) on the sodium current were compared with those of a typical scorpion alpha-toxin and the spider d-palutoxins and d-atracotoxins on insect Nav channels. Tx4(6-1) appears to be insect selective, being ineffective on mammalian Nav channels [83]. Recently, another sodium channel neurotoxin from the venom of the Chinese bird spider S. huwena, which has been named huwentoxin IV, was described [84].…”

Section: Spptxs Acting On Sodium Channelsmentioning

confidence: 99%

Pharmacologically active spider peptide toxins

Corzo

Escoubas

2003

Cellular and Molecular Life Sciences (CMLS)

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Advances in mass spectrometry and peptide biochemistry coupled to modern methods in electrophysiology have permitted the isolation and identification of numerous novel peptide toxins from animal venoms in recent years. These advances have also opened up the field of spider venom research, previously unexplored due to methodological limitations. Many peptide toxins from spider venoms share structural features, amino acid composition and consensus sequences that allow them to interact with related classes of cellular receptors. They have become increasingly useful agents for the study of voltage-sensitive and ligand-gated ion channels and the discrimination of their cellular subtypes. Spider peptide toxins have also been recognized as useful agents for their antimicrobial properties and the study of pore formation in cell membranes. Spider peptide toxins with nanomolar affinities for their receptors are thus promising pharmacological tools for understanding the physiological role of ion channels and as leads for the development of novel therapeutic agents and strategies for ion channel-related diseases. Their high insecticidal potency can also make them useful probes for the discovery of novel insecticide targets in the insect nervous system or for the development of genetically engineered microbial pesticides.

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“…Patch clamp experiments on Nav1.2 and Nav1.4 channels expressed in Xenopus oocytes revealed that Tx4(6-1) failed to alter any aspects of Nav channel gating or kinetics indicating that this toxin appears to be insect-selective (de Lima et al, 2002). Given these insect-selective actions on site 3 it is not surprising that the toxin has been found to compete with the scorpion α-like toxin Bom IV for site 3 on insect Nav channels (de Lima et al, 2002). Thus Tx4(6-1) together with Magi 2 represents a growing family of excitatory insect-selective spider neurotoxins targeting site 3 on the Nav channel.…”

Section: Nicholson and Little !mentioning

confidence: 98%

SPider Neurotoxins Targeting Voltage-Gated Sodium Channels

Nicholson¹,

Little²

2005

Toxin Revs.

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The voltage-gated sodium (Nav) channel is a target for a number of drugs, insecticides and neurotoxins. These bind to at least seven identified neurotoxin binding sites and either block conductance or modulate sodium channel gating and / or kinetics. A number of polypeptide toxins from the venoms of araneomorph and mygalomorph spiders have been isolated and characterized that interact with several of these sites. Certain huwentoxins and hainantoxins appear to target site 1 to block Nav channel conductance. The δ-atracotoxins and Magi 4 slow Nav channel inactivation via an interaction with neurotoxin site 3. The δ-palutoxins, and most likely µ-agatoxins and curtatoxins, target site 4. However their action is complex with the µ-agatoxins causing a hyperpolarizing shift the voltage-dependence of activation, an action analogous to scorpion β-toxins, but with both δ-palutoxins and µ-agatoxins slowing Nav channel inactivation, a site 3 like action. Many spider toxins target undefined sites, while others are likely to cross-react with other ion channels due to conservedstructures within domains of voltage-gated ion channels. It is already clear, however, that many spider toxins represent highly potent and specific molecular tools to define novel links between sites modulating channel activation and inactivation. Other spider toxins show phyla-specificity and are being considered as lead compounds for the development of biopesticides. Others display tissue specificity via interactions with specific Nav channel subtypes and should provide useful tools to delineate the molecular determinants to target ligands to these channel subtypes. These studies are being greatly assisted by the determination of the pharmacophore of these toxins, but without precise identification of their binding site and mode of action their potential in the above areas remains underdeveloped.!

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The toxin Tx4(6-1) from the spider Phoneutria nigriventer slows down Na+ current inactivation in insect CNS via binding to receptor site 3

Cited by 54 publications

References 38 publications

Structure of Membrane-active Toxin from Crab Spider Heriaeus melloteei Suggests Parallel Evolution of Sodium Channel Gating Modifiers in Araneomorphae and Mygalomorphae

Structure of Membrane-active Toxin from Crab Spider Heriaeus melloteei Suggests Parallel Evolution of Sodium Channel Gating Modifiers in Araneomorphae and Mygalomorphae

Pharmacologically active spider peptide toxins

SPider Neurotoxins Targeting Voltage-Gated Sodium Channels

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