Natural inhibitors of snake venom toxins: a promising source of therapeutic peptides for toxin-centric next-generation antivenoms

Present review article explains ant venom components and its allergic and biological effects in man and animals. Red ants or small fire ants secrete and inject venom very swiftly to defend their nest against predators, microbial pathogens, and competitors and to hunt the prey. Ant venom is a mixture of various organic compounds, including peptides, enzymes, and polypeptide toxins. It is highly toxic, allergic, invasive and venomous. It imposes sever paralytic, cytolytic, haemolytic, allergenic, pro-inflammatory, insecticidal, antimicrobial, and pain-producing pharmacologic activities after infliction. Victims show red ring-shaped allergic sign with regional swelling marked with intense pain. Ant venom also contains several hydrolases, oxidoreductases, proteases, Kunitz-like polypeptides, and inhibitor cysteine knot (ICK)-like (knottin) neurotoxins and insect defensins. Ant venom toxins/proteins generate allergic immune responses and employ eosinophils and produce Th2 cytokines, response. These compounds from ant venom could be used as a potential source of new anticonvulsants molecules. Ant venoms contain many small, linear peptides, an untapped source of bioactive peptide toxins. The remarkable insecticidal activity of ant venom could be used as a promising source of additional bio-insecticides and therapeutic agents.

Download Full-text

Snake venom toxins—II. The primary structures of cytotoxin homologues S3C2 and S4C8 from Aspidelaps scutatus (shield or shield-nose snake) venom

International Journal of Biochemistry ◽

10.1016/0020-711x(88)90361-8 ◽

1988 ◽

Vol 20 (3) ◽

pp. 337-345 ◽

Cited By ~ 3

Author(s):

Francois J. Joubert

Keyword(s):

Snake Venom ◽

Venom Toxins ◽

Primary Structures

Download Full-text

Snake Venom Toxins Targeted at the Nervous System

Snake Venoms ◽

10.1007/978-94-007-6648-8_23-1 ◽

2015 ◽

pp. 1-21 ◽

Cited By ~ 1

Author(s):

Alexey V. Osipov ◽

Yuri N. Utkin

Keyword(s):

Nervous System ◽

Snake Venom ◽

Venom Toxins

Download Full-text

Natural Inhibitors of Snake Venom Metallopeptidases

Toxins and Drug Discovery - Toxinology ◽

10.1007/978-94-007-6452-1_19 ◽

2017 ◽

pp. 53-80

Author(s):

Ana G. C. Neves-Ferreira ◽

Richard H. Valente ◽

Gilberto B. Domont ◽

Jonas Perales

Keyword(s):

Snake Venom ◽

Natural Inhibitors

Download Full-text

Varespladib Inhibits the Phospholipase A2 and Coagulopathic Activities of Venom Components from Hemotoxic Snakes

Biomedicines ◽

10.3390/biomedicines8060165 ◽

2020 ◽

Vol 8 (6) ◽

pp. 165 ◽

Cited By ~ 2

Author(s):

Chunfang Xie ◽

Laura-Oana Albulescu ◽

Kristina B. M. Still ◽

Julien Slagboom ◽

Yumei Zhao ◽

...

Keyword(s):

Phospholipase A2 ◽

Snake Venom ◽

Snake Venoms ◽

Venom Toxins ◽

Inhibitory Molecule ◽

Coagulation Assay ◽

Potential Clinical Utility ◽

Bothrops Asper ◽

Echis Carinatus ◽

Deinagkistrodon Acutus

Phospholipase A2 (PLA2) enzymes are important toxins found in many snake venoms, and they can exhibit a variety of toxic activities including causing hemolysis and/or anticoagulation. In this study, the inhibiting effects of the small molecule PLA2 inhibitor varespladib on snake venom PLA2s was investigated by nanofractionation analytics, which combined chromatography, mass spectrometry (MS), and bioassays. The venoms of the medically important snake species Bothrops asper, Calloselasma rhodostoma, Deinagkistrodon acutus, Daboia russelii, Echis carinatus, Echis ocellatus, and Oxyuranus scutellatus were separated by liquid chromatography (LC) followed by nanofractionation and interrogation of the fractions by a coagulation assay and a PLA2 assay. Next, we assessed the ability of varespladib to inhibit the activity of enzymatic PLA2s and the coagulopathic toxicities induced by fractionated snake venom toxins, and identified these bioactive venom toxins and those inhibited by varespladib by using parallel recorded LC-MS data and proteomics analysis. We demonstrated here that varespladib was not only capable of inhibiting the PLA2 activities of hemotoxic snake venoms, but can also effectively neutralize the coagulopathic toxicities (most profoundly anticoagulation) induced by venom toxins. While varespladib effectively inhibited PLA2 toxins responsible for anticoagulant effects, we also found some evidence that this inhibitory molecule can partially abrogate procoagulant venom effects caused by different toxin families. These findings further emphasize the potential clinical utility of varespladib in mitigating the toxic effects of certain snakebites.

Download Full-text

A plea for standardized nomenclature of snake venom toxins

Toxicon ◽

10.1016/j.toxicon.2014.08.070 ◽

2014 ◽

Vol 90 ◽

pp. 351-353 ◽

Cited By ~ 2

Author(s):

Adam D. Hargreaves ◽

John F. Mulley

Keyword(s):

Snake Venom ◽

Venom Toxins

Download Full-text