Brown Spider Venom Phospholipase-D Activity upon Different Lipid Substrates

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Autor(es): dc.contributorUniversidade Federal do Paraná (UFPR)-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversidade Estadual de Ponta Grossa (UEPG)-
Autor(es): dc.contributorUniversity of California San Diego-
Autor(es): dc.creatorChaves-Moreira, Daniele-
Autor(es): dc.creatorGremski, Luiza Helena-
Autor(es): dc.creatorde Moraes, Fábio Rogério-
Autor(es): dc.creatorVuitika, Larissa-
Autor(es): dc.creatorWille, Ana Carolina Martins-
Autor(es): dc.creatorHernández González, Jorge Enrique-
Autor(es): dc.creatorChaim, Olga Meiri-
Autor(es): dc.creatorSenff-Ribeiro, Andrea-
Autor(es): dc.creatorArni, Raghuvir Krishnaswamy-
Autor(es): dc.creatorVeiga, Silvio Sanches-
Data de aceite: dc.date.accessioned2025-08-21T15:33:47Z-
Data de disponibilização: dc.date.available2025-08-21T15:33:47Z-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-01-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3390/toxins15020109-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/249715-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/249715-
Descrição: dc.descriptionBrown spider envenomation results in dermonecrosis, characterized by an intense inflammatory reaction. The principal toxins of brown spider venoms are phospholipase-D isoforms, which interact with different cellular membrane components, degrade phospholipids, and generate bioactive mediators leading to harmful effects. The Loxosceles intermedia phospholipase D, LiRecDT1, possesses a loop that modulates the accessibility to the active site and plays a crucial role in substrate. In vitro and in silico analyses were performed to determine aspects of this enzyme’s substrate preference. Sphingomyelin d18:1/6:0 was the preferred substrate of LiRecDT1 compared to other Sphingomyelins. Lysophosphatidylcholine 16:0/0:0 was preferred among other lysophosphatidylcholines, but much less than Sphingomyelin d18:1/6:0. In contrast, phosphatidylcholine d18:1/16:0 was not cleaved. Thus, the number of carbon atoms in the substrate plays a vital role in determining the optimal activity of this phospholipase-D. The presence of an amide group at C2 plays a key role in recognition and activity. In silico analyses indicated that a subsite containing the aromatic residues Y228 and W230 appears essential for choline recognition by cation-π interactions. These findings may help to explain why different cells, with different phospholipid fatty acid compositions exhibit distinct susceptibilities to brown spider venoms.-
Descrição: dc.descriptionDepartment of Cell Biology Federal University of Paraná (UFPR)-
Descrição: dc.descriptionDepartment of Physics Multi-User Center for Biomolecular Innovation State University of São Paulo (UNESP)-
Descrição: dc.descriptionDepartment of Structural and Molecular Biology State University of Ponta Grossa (UEPG)-
Descrição: dc.descriptionDepartment of Pharmacology University of California San Diego, La Jolla-
Descrição: dc.descriptionDepartment of Physics Multi-User Center for Biomolecular Innovation State University of São Paulo (UNESP)-
Idioma: dc.languageen-
Relação: dc.relationToxins-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectbrown spider-
Palavras-chave: dc.subjectLoxosceles intermedia-
Palavras-chave: dc.subjectphospholipase-D substrate-
Palavras-chave: dc.subjectphospholipids-
Palavras-chave: dc.subjectrecombinant toxin-
Palavras-chave: dc.subjectvenom-
Título: dc.titleBrown Spider Venom Phospholipase-D Activity upon Different Lipid Substrates-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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