Two new arthropod toxins purified from the venom of the Mexican scorpion Centruroides nigrescens

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  Two new arthropod toxins purified from the venom of the Mexican scorpion Centruroides nigrescens Abstract The venom of the slender black scorpion Centruroides nigrescens , from the State of Guerrero México, was fractionated by Sephadex G–50 gel filtration, followed by carboxymethyl cellulose ion separation and high–performance liquid chromatography, permitting to obtain two new peptides toxic to arthropods. The estimate LD 50 of the soluble venom for the insect Acheta domesticus was 11.1 μg/g body weight, and for the arthropod Armadillidium vulgare was 61.1 μg body weight . The amino acid sequence of toxin Cnige1 (toxic to A. domesticus and A. vulgare ) contains 65 amino acids, with a molecular mass of 7273.37 mass units, whereas toxin Cnige2, toxic to A. domesticus , contains 68 amino acids, with a molecular mass of 7548.81 units. Both peptides are well packed, containing 8 cysteines, which in the native venoms are forming 4 disulfide bridges each. The amino acid sequences f...

Comparative Biochemical, Structural, and Functional Analysis of Recombinant Phospholipases D from Three Loxosceles Spider Venoms

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Comparative Biochemical, Structural, and Functional Analysis of Recombinant Phospholipases D from Three Loxosceles Spider Venoms

Abstract

Spiders of Loxosceles genus are widely distributed and their venoms contain phospholipases D (PLDs), which degrade phospholipids and trigger inflammatory responses, dermonecrosis, hematological changes, and renal injuries. Biochemical, functional, and structural properties of three recombinant PLDs from L. intermedia, L. laeta, and L. gaucho, the principal species clinically relevant in South America, were analyzed. Sera against L. gaucho and L. laeta PLDs strongly cross-reacted with other PLDs, but sera against L. intermedia PLD mostly reacted with homologous molecules, suggesting underlying structural and functional differences. PLDs presented a similar secondary structure profile but distinct melting temperatures. Different methods demonstrated that all PLDs cleave sphingomyelin and lysophosphatidylcholine, but L. gaucho and L. laeta PLDs excelled. L. gaucho PLD showed greater “in vitro” hemolytic activity. L. gaucho and L. laeta PLDs were more lethal in assays with mice and crickets. Molecular dynamics simulations correlated their biochemical activities with differences in sequences and conformations of specific surface loops, which play roles in protein stability and in modulating interactions with the membrane. Despite the high similarity, PLDs from L. gaucho and L. laeta venoms are more active than L. intermedia PLD, requiring special attention from physicians when these two species prevail in endemic regions.

da Justa, Hanna Câmara, Jorge Enrique Hernández González, Larissa Vuitika, Ricardo Barros Mariutti, Pedro Augusto Martinho Magnago, Fábio Rogério de Moraes, Andrea Senff-Ribeiro, Luiza Helena Gremski, Raghuvir Krishnaswamy Arni, and Silvio Sanches Veiga. 2023. "Comparative Biochemical, Structural, and Functional Analysis of Recombinant Phospholipases D from Three Loxosceles Spider Venoms" International Journal of Molecular Sciences 24, no. 15: 12006. https://doi.org/10.3390/ijms241512006