Brown Spider Venom Phospholipase-D Activity upon Different Lipid Substrates

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dc.contributor.authorChaves-Moreira, Daniele
dc.contributor.authorGremski, Luiza Helena
dc.contributor.authorde Moraes, Fábio Rogério [UNESP]
dc.contributor.authorVuitika, Larissa
dc.contributor.authorWille, Ana Carolina Martins
dc.contributor.authorHernández González, Jorge Enrique [UNESP]
dc.contributor.authorChaim, Olga Meiri
dc.contributor.authorSenff-Ribeiro, Andrea
dc.contributor.authorArni, Raghuvir Krishnaswamy [UNESP]
dc.contributor.authorVeiga, Silvio Sanches
dc.contributor.institutionUniversidade Federal do Paraná (UFPR)
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionUniversidade Estadual de Ponta Grossa (UEPG)
dc.contributor.institutionUniversity of California San Diego
dc.date.accessioned2023-07-29T16:07:18Z
dc.date.available2023-07-29T16:07:18Z
dc.date.issued2023-02-01
dc.description.abstractBrown 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.en
dc.description.affiliationDepartment of Cell Biology Federal University of Paraná (UFPR)
dc.description.affiliationDepartment of Physics Multi-User Center for Biomolecular Innovation State University of São Paulo (UNESP)
dc.description.affiliationDepartment of Structural and Molecular Biology State University of Ponta Grossa (UEPG)
dc.description.affiliationDepartment of Pharmacology University of California San Diego, La Jolla
dc.description.affiliationUnespDepartment of Physics Multi-User Center for Biomolecular Innovation State University of São Paulo (UNESP)
dc.identifierhttp://dx.doi.org/10.3390/toxins15020109
dc.identifier.citationToxins, v. 15, n. 2, 2023.
dc.identifier.doi10.3390/toxins15020109
dc.identifier.issn2072-6651
dc.identifier.scopus2-s2.0-85149197149
dc.identifier.urihttp://hdl.handle.net/11449/249715
dc.language.isoeng
dc.relation.ispartofToxins
dc.sourceScopus
dc.subjectbrown spider
dc.subjectLoxosceles intermedia
dc.subjectphospholipase-D substrate
dc.subjectphospholipids
dc.subjectrecombinant toxin
dc.subjectvenom
dc.titleBrown Spider Venom Phospholipase-D Activity upon Different Lipid Substratesen
dc.typeArtigo
unesp.author.orcid0000-0001-6562-8817[1]
unesp.author.orcid0000-0002-0425-0352[3]
unesp.author.orcid0000-0002-4770-8677[6]
unesp.author.orcid0000-0002-3854-3292[7]
unesp.author.orcid0000-0002-7967-6307[8]
unesp.author.orcid0000-0003-2460-1145[9]

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