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From Animal Venoms to Solutions: In Honor of Professor Lourival...
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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: 15 February 2025 | Viewed by 4953

Special Issue Editor

Prof. Dr. Elisabeth Ferroni Schwartz

E-Mail Website
Guest Editor
Department of Physiological Sciences, Institute of Biological Sciences, University of Brasilia, Brasilia 70910-900, DF, Brazil
Interests: ion channel; scorpion venom; theraphosidae venom; neurotoxins
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

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

Manuscript Submission Information

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Keywords

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

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Published Papers (5 papers)

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Research

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11 pages, 3032 KiB  
Article
Evaluating a Venom-Bioinspired Peptide, NOR-1202, as an Antiepileptic Treatment in Male Mice Models
by Maria Varela Torres Quintanilha, Giovanna de Azevedo Mello Gobbo, Gabriela Beserra Pinheiro, Adolfo Carlos Barros de Souza, Luana Cristina Camargo and Marcia Renata Mortari
Toxins 2024, 16(8), 342; https://doi.org/10.3390/toxins16080342 - 5 Aug 2024
Viewed by 437
Abstract
Epilepsy, a neurological disorder characterized by excessive neuronal activity and synchronized electrical discharges, ranks among the most prevalent global neurological conditions. Despite common use, antiepileptic drugs often result in adverse effects and lack effectiveness in controlling seizures in temporal lobe epilepsy (TLE) patients. [...] Read more.
Epilepsy, a neurological disorder characterized by excessive neuronal activity and synchronized electrical discharges, ranks among the most prevalent global neurological conditions. Despite common use, antiepileptic drugs often result in adverse effects and lack effectiveness in controlling seizures in temporal lobe epilepsy (TLE) patients. Recent research explored the potential of occidentalin-1202, a peptide inspired by Polybia occidentalis venom, in safeguarding Wistar rats from chemically induced seizures. The present study evaluated the new analog from occidentalin-1202 named NOR-1202 using acute and chronic pilocarpine-induced models and an acute kainic acid (KA) male mice model. NOR-1202 was administered through the intracerebroventricular (i.c.v.), subcutaneous, or intraperitoneal routes, with stereotaxic procedures for the i.c.v. injection. In the acute pilocarpine-induced model, NOR-1202 (i.c.v.) protected against generalized seizures and mortality but lacked systemic antiepileptic activity. In the KA model, it did not prevent generalized seizures but improved survival. In the chronic TLE model, NOR-1202′s ED50 did not differ significantly from the epileptic or healthy groups regarding time spent in spontaneous recurrent seizures during the five-day treatment. However, the NOR-1202 group exhibited more seizures than the healthy group on the second day of treatment. In summary, NOR-1202 exhibits antiepileptic effects against chemoconvulsant-induced seizures, but no effect was observed when administered systemically. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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15 pages, 2994 KiB  
Article
Venomics of Scorpion Ananteris platnicki (Lourenço, 1993), a New World Buthid That Inhabits Costa Rica and Panama
by Cecilia Díaz, Bruno Lomonte, Arturo Chang-Castillo, Fabián Bonilla, Adriana Alfaro-Chinchilla, Felipe Triana, Diego Angulo, Julián Fernández and Mahmood Sasa
Toxins 2024, 16(8), 327; https://doi.org/10.3390/toxins16080327 - 23 Jul 2024
Viewed by 500
Abstract
Ananteris is a scorpion genus that inhabits dry and seasonal areas of South and Central America. It is located in a distinctive morpho-group of Buthids, the ‘Ananteris group’, which also includes species distributed in the Old World. Because of the lack of [...] Read more.
Ananteris is a scorpion genus that inhabits dry and seasonal areas of South and Central America. It is located in a distinctive morpho-group of Buthids, the ‘Ananteris group’, which also includes species distributed in the Old World. Because of the lack of information on venom composition, the study of Ananteris species could have biological and medical relevance. We conducted a venomics analysis of Ananteris platnicki, a tiny scorpion that inhabits Panama and Costa Rica, which shows the presence of putative toxins targeting ion channels, as well as proteins with similarity to hyaluronidases, proteinases, phospholipases A2, members of the CAP-domain family, and hemocyanins, among others. Venom proteolytic and hyaluronidase activities were corroborated. The determination of the primary sequences carried out by mass spectrometry evidences that several peptides are similar to the toxins present in venoms from Old World scorpion genera such as Mesobuthus, Lychas, and Isometrus, but others present in Tityus and Centruroides toxins. Even when this venom displays the characteristic protein families found in all Buthids, with a predominance of putative Na+-channel toxins and proteinases, some identified partial sequences are not common in venoms of the New World species, suggesting its differentiation into a distinctive group separated from other Buthids. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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19 pages, 3821 KiB  
Article
Unveiling Tst3, a Multi-Target Gating Modifier Scorpion α Toxin from Tityus stigmurus Venom of Northeast Brazil: Evaluation and Comparison with Well-Studied Ts3 Toxin of Tityus serrulatus
by Diogo Vieira Tibery, João Antonio Alves Nunes, Daniel Oliveira da Mata, Luis Felipe Santos Menezes, Adolfo Carlos Barros de Souza, Matheus de Freitas Fernandes-Pedrosa, Werner Treptow and Elisabeth Ferroni Schwartz
Toxins 2024, 16(6), 257; https://doi.org/10.3390/toxins16060257 - 3 Jun 2024
Viewed by 695
Abstract
Studies on the interaction sites of peptide toxins and ion channels typically involve site-directed mutations in toxins. However, natural mutant toxins exist among them, offering insights into how the evolutionary process has conserved crucial sequences for activities and molecular target selection. In this [...] Read more.
Studies on the interaction sites of peptide toxins and ion channels typically involve site-directed mutations in toxins. However, natural mutant toxins exist among them, offering insights into how the evolutionary process has conserved crucial sequences for activities and molecular target selection. In this study, we present a comparative investigation using electrophysiological approaches and computational analysis between two alpha toxins from evolutionarily close scorpion species of the genus Tityus, namely, Tst3 and Ts3 from T. stigmurus and T. serrulatus, respectively. These toxins exhibit three natural substitutions near the C-terminal region, which is directly involved in the interaction between alpha toxins and Nav channels. Additionally, we characterized the activity of the Tst3 toxin on Nav1.1-Nav1.7 channels. The three natural changes between the toxins did not alter sensitivity to Nav1.4, maintaining similar intensities regarding their ability to alter opening probabilities, delay fast inactivation, and induce persistent currents. Computational analysis demonstrated a preference for the down conformation of VSD4 and a shift in the conformational equilibrium towards this state. This illustrates that the sequence of these toxins retained the necessary information, even with alterations in the interaction site region. Through electrophysiological and computational analyses, screening of the Tst3 toxin on sodium isoform revealed its classification as a classic α-NaTx with a broad spectrum of activity. It effectively delays fast inactivation across all tested isoforms. Structural analysis of molecular energetics at the interface of the VSD4-Tst3 complex further confirmed this effect. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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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 - 1 Mar 2024
Cited by 1 | Viewed by 1506
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
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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Review

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22 pages, 2744 KiB  
Review
Shining a Light on Venom-Peptide Receptors: Venom Peptides as Targeted Agents for In Vivo Molecular Imaging
by Chun Yuen Chow and Glenn F. King
Toxins 2024, 16(7), 307; https://doi.org/10.3390/toxins16070307 - 4 Jul 2024
Viewed by 1119
Abstract
Molecular imaging has revolutionised the field of biomedical research by providing a non-invasive means to visualise and understand biochemical processes within living organisms. Optical fluorescent imaging in particular allows researchers to gain valuable insights into the dynamic behaviour of a target of interest [...] Read more.
Molecular imaging has revolutionised the field of biomedical research by providing a non-invasive means to visualise and understand biochemical processes within living organisms. Optical fluorescent imaging in particular allows researchers to gain valuable insights into the dynamic behaviour of a target of interest in real time. Ion channels play a fundamental role in cellular signalling, and they are implicated in diverse pathological conditions, making them an attractive target in the field of molecular imaging. Many venom peptides exhibit exquisite selectivity and potency towards ion channels, rendering them ideal agents for molecular imaging applications. In this review, we illustrate the use of fluorescently-labelled venom peptides for disease diagnostics and intraoperative imaging of brain tumours and peripheral nerves. Finally, we address challenges for the development and clinical translation of venom peptides as nerve-targeted imaging agents. Full article
(This article belongs to the Special Issue From Animal Venoms to Solutions: In Honor of Professor Lourival D. Possani on the Occasion of His 85th Birthday)
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