New Insights into Structure and Function of Arthropod Toxins and Other Toxins: Tribute to Professor Hervé Rochat

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

Deadline for manuscript submissions: 31 July 2024 | Viewed by 2153

Special Issue Editors


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Guest Editor
Faculdade Santa Casa de Belo Horizonte – Programa de Pós Graduação em Medicina e Biomedicina, Belo Horizonte, Brazil
Interests: toxins; biotechnology; spider venom; antimicrobial toxins; toxins and pain; anticancer toxins; toxins and therapeutic; arthropod toxins; animal venoms; toxin active in erectile function
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Guest Editor
CNRS, UMR 7275, IPMC, 660 Route des Lucioles, 06560 Valbonne-Sophia Antipolis, France
Interests: functional studies of voltage-gated sodium channel mutations implicated in migraine; epilepsy; autism and intellectual disability

Special Issue Information

Dear Colleagues,

This Special Issue is in honor of the late Professor Hervé Rochat. It aims to showcase new research on the structure and function of different venoms, especially arthropod venoms. Professor Hervé Rochat, who passed away in January 2023, was a pioneer in the field of toxins and was passionate about it throughout his scientific career. The work accomplished in his lab has been an inspiration for many scientists around the world. It has allowed key discoveries not only on the structure–function relationship of animal toxins, but also on the function of their targets, particularly ion channels. His lab has developed several skills to tackle the understanding of the structure–function relationship of toxins, starting from a biochemical point of view: purification, amino acid analysis and elucidation of the primary, secondary and tertiary structures. Subsequently, more insights were obtained with pharmacological and immunological experiments. It is important to point out that Prof. Hervé Rochat’s laboratory developed cutting-edge techniques that enabled innovative and outstanding research to be conducted. For these reasons, Prof. Hervé Rochat attracted researchers and students from all the continents by contributing to their training practices. Moreover, being a great mentor, he supported these researchers to pursue these studies in their countries and to develop their own laboratories. Many of us are glad for being part of his team and are grateful for his immense support. We believe that good science lives and evolves through generations and that our role is to pursue it, drawing inspiration from our masters. This is certainly the main tribute we can pay to them.

Prof. Dr. Maria Elena De Lima
Dr. Sandrine Cestèle
Guest Editors

Manuscript Submission Information

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Keywords

  • peptide
  • venom
  • toxin
  • ion channels

Published Papers (1 paper)

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Review

19 pages, 1297 KiB  
Review
Jelleine, a Family of Peptides Isolated from the Royal Jelly of the Honey Bees (Apis mellifera), as a Promising Prototype for New Medicines: A Narrative Review
by William Gustavo Lima, Julio Cesar Moreira Brito, Rodrigo Moreira Verly and Maria Elena de Lima
Toxins 2024, 16(1), 24; https://doi.org/10.3390/toxins16010024 - 02 Jan 2024
Viewed by 1817
Abstract
The jelleine family is a group of four peptides (jelleines I–IV) originally isolated from the royal jelly of honey bee (Apis mellifera), but later detected in some honey samples. These oligopeptides are composed of 8–9 amino acid residues, positively charged (+2 [...] Read more.
The jelleine family is a group of four peptides (jelleines I–IV) originally isolated from the royal jelly of honey bee (Apis mellifera), but later detected in some honey samples. These oligopeptides are composed of 8–9 amino acid residues, positively charged (+2 to +3 at pH 7.2), including 38–50% of hydrophobic residues and a carboxamide C-terminus. Jelleines, generated by processing of the C-terminal region of major royal jelly proteins 1 (MRJP-1), play an important biological role in royal jelly conservation as well as in protecting bee larvae from potential pathogens. Therefore, these molecules present numerous benefits for human health, including therapeutic purposes as shown in preclinical studies. In this review, we aimed to evaluate the biological effects of jelleines in addition to characterising their toxicities and stabilities. Jelleines I–III have promising antimicrobial activity and low toxicity (LD50 > 1000 mg/Kg). However, jelleine-IV has not shown relevant biological potential. Jelleine-I, but not the other analogues, also has antiparasitic, healing, and pro-coagulant activities in addition to indirectly modulating tumor cell growth and controlling the inflammatory process. Although it is sensitive to hydrolysis by proteases, the addition of halogens increases the chemical stability of these molecules. Thus, these results suggest that jelleines, especially jelleine-I, are a potential target for the development of new, effective and safe therapeutic molecules for clinical use. Full article
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