From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: 9 July 2024 | Viewed by 1375

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Department of Physiological Sciences, Institute of Biological Sciences, University of Brasilia, Brasilia 70910-900, DF, Brazil
Interests: ion channel; scorpion venom; theraphosidae venom; neurotoxins
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Dear Colleagues,

It has not been precisely determined when humans started to use animal venoms for medicinal purposes. Thousands of years ago, animal venoms were the basis of preparations used as treatments for smallpox, leprosy, fever and wound healing. In the 1st century AD, a mixture named theriac, or theriaca, which contained leaven, honey and the flesh of venomous animals, including that of scorpions and viper snakes, was developed by Greeks and used by Romans, as well as in Persia, China and India. Historical data indicate that even the Roman emperor Marcus Aurelius took it on a regular basis. Theriac was used until the 18th century.

The history of the prospection of venom compounds also traces back more than two millennia.

Venom glands, injection apparatus and noxious secretions have evolved in animals for the capture of prey and for defense purposes. Venomous vertebrates and invertebrates possess exocrine cells or glands that produce energetically expensive, highly efficient and complex mixtures, whose compositions depend on the venomous species. Snakes, spiders, scorpions, bees, wasps, anemones, cone snails and jellyfishes are the most commonly studied venomous animals.

Mainly due to its medical significance, many studies comprise the effects of whole venom, the mechanism of action of the main toxins and the search for specific human envenoming treatment. Bites or stings by certain venomous species result in severe envenomation and high mortality rates. The most effective treatment to date is the use of injectable antivenoms.

Besides the health-related importance regarding human envenoming, venom-related research relating to the search for new compounds that are potential templates for the development of new pharmacological tools and medicines has been growing fast in recent decades. For instance, the long evolution process, the distribution to almost all environments and the diversity of prey and predators resulted in very complex venoms that contain molecules with unique biological properties, which can be used in both basic science and clinical applications.

Over the past five decades, many researchers have studied animal venoms. Prof. Lourival D Possani deserves to be highlighted for his broad contributions in the area, particularly his significant contributions to the completion of the first original works that describe scorpion toxins as modifiers of the function of different ion channels and for the discovery of two new antibiotics. During the period 1971–1973, he completed a postdoctoral stay in the laboratory of Dr. Edward Reich at Rockefeller University, NY, USA, where he worked with components of animal venoms and participated in the isolation of the acetylcholine receptor. In 1974, he began his academic career in Mexico at the Institute of Biology of the UNAM, working on aspects related to the functioning of GABAergic neurons in the group of Dr. Ricardo Tapia. Shortly after, he recognized that Mexico had a public health problem regarding scorpion stings and that the molecular identities of the components of their venoms and their molecular mechanism of action were unknown. Thus, Prof. Possani formed his research group with the objective of characterizing the components of scorpion venoms. In 2024, he will turn 85 years old, and Toxins has decided to pay tribute with a special edition.

The Toxins Special Issue entitled “From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday” intends to amalgamate high-quality, original, basic and clinical research articles by established academic authors as well as new researchers. Articles reporting research data obtained in the field of animal venom and covering a wide range of topics including human envenoming, antivenoms, venom compounds, their mechanism of action and the prospection of new drugs from animal venoms will be published.

Prof. Dr. Elisabeth Ferroni Schwartz
Guest Editor

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Keywords

  • venom
  • snake
  • spider
  • scorpion
  • toxins
  • antivenom
  • venom prospection
  • anemone
  • conus
  • ant
  • bee
  • wasp
  • jellyfish
  • stingrays
  • lonomia
  • tarantula
  • viper

Published Papers (1 paper)

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14 pages, 8459 KiB  
Article
Characterization of Sodium Channel Peptides Obtained from the Venom of the Scorpion Centruroides bonito
by Rita Restano-Cassulini, Timoteo Olamendi-Portugal, Lidia Riaño-Umbarila, Fernando Z. Zamudio, Gustavo Delgado-Prudencio, Baltazar Becerril and Lourival D. Possani
Toxins 2024, 16(3), 125; https://doi.org/10.3390/toxins16030125 - 01 Mar 2024
Viewed by 1059
Abstract
Five peptides were isolated from the venom of the Mexican scorpion Centruroides bonito by chromatographic procedures (molecular weight sieving, ion exchange columns, and HPLC) and were denoted Cbo1 to Cbo5. The first four peptides contain 66 amino acid residues and the last one [...] Read more.
Five peptides were isolated from the venom of the Mexican scorpion Centruroides bonito by chromatographic procedures (molecular weight sieving, ion exchange columns, and HPLC) and were denoted Cbo1 to Cbo5. The first four peptides contain 66 amino acid residues and the last one contains 65 amino acids, stabilized by four disulfide bonds, with a molecular weight spanning from about 7.5 to 7.8 kDa. Four of them are toxic to mice, and their function on human Na+ channels expressed in HEK and CHO cells was verified. One of them (Cbo5) did not show any physiological effects. The ones toxic to mice showed that they are modifiers of the gating mechanism of the channels and belong to the beta type scorpion toxin (β-ScTx), affecting mainly the Nav1.6 channels. A phylogenetic tree analysis of their sequences confirmed the high degree of amino acid similarities with other known bona fide β-ScTx. The envenomation caused by this venom in mice is treated by using commercially horse antivenom available in Mexico. The potential neutralization of the toxic components was evaluated by means of surface plasmon resonance using four antibody fragments (10FG2, HV, LR, and 11F) which have been developed by our group. These antitoxins are antibody fragments of single-chain antibody type, expressed in E. coli and capable of recognizing Cbo1 to Cbo4 toxins to various degrees. Full article
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