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Review

Understanding the complexity of Tityus serrulatus venom: A focus on high molecular weight components

Isadora Sousa de Oliveira1,2, Nicoly Malachize Alano-da-Silva1, Isabela Gobbo Ferreira1, Felipe Augusto Cerni3, Jacqueline de Almeida Gonçalves Sachett4,5, Wuelton Marcelo Monteiro4,5, Manuela Berto Pucca6, Eliane Candiani Arantes1* [ + show more ]

J Venom Anim Toxins incl Trop Dis, 2024, 30:e20230046
Received: 25 July 2023 | Accepted: 04 December 2023 | Published online: 22 January 2024
Collection: Spotlighting toxinology: from animal toxins to next-generation technologies and products
https://doi.org/10.1590/1678-9199-JVATITD-2023-0046

Abstract

Tityus serrulatus scorpion is responsible for a significant number of envenomings in Brazil, ranging from mild to severe, and in some cases, leading to fatalities. While supportive care is the primary treatment modality, moderate and severe cases require antivenom administration despite potential limitations and adverse effects. The remarkable proliferation of T. serrulatus scorpions, attributed to their biology and asexual reproduction, contributes to a high incidence of envenomation. T. serrulatus scorpion venom predominantly consists of short proteins acting as neurotoxins (α and β), that primarily target ion channels. Nevertheless, high molecular weight compounds, including metalloproteases, serine proteases, phospholipases, and hyaluronidases, are also present in the venom. These compounds play a crucial role in envenomation, influencing the severity of symptoms and the spread of venom. This review endeavors to comprehensively understand the T. serrulatus scorpion venom by elucidating the primary high molecular weight compounds and exploring their potential contributions to envenomation. Understanding these compounds’ mechanisms of action can aid in developing more effective treatments and prevention strategies, ultimately mitigating the impact of scorpion envenomation on public health in Brazil.

 

Keywords: Tityus serrulatus; Proteases; Hyaluronidase; Phospholipase; Cysteine-rich secretory proteins

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