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Antivenomic approach of different Crotalus durissus collilineatus venoms J. Venom. Anim. Toxins incl. Trop. Dis.
Oliveira,Isadora Sousa de; Pucca,Manuela Berto; Sampaio,Suely Vilela; Arantes,Eliane Candiani.
Abstract Background: Our group has previously performed a proteomic study verifying that individual variations can occur among Crotalus durissus collilineatus venoms. These variations may lead to differences in venom toxicity and may result in lack of neutralization of some components by antivenom. In this way, this study aimed to evaluate the Brazilian anticrotalic serum capacity in recognizing twenty-two Crotalus durissus collilineatus venoms, as well as their fractions. Methods: The indirect enzyme-linked immunosorbent assay (ELISA) was chosen to evaluate the efficacy of heterologous anticrotalic serum produced by Instituto Butantan (Brazil) in recognizing the twenty-two Crotalus durissus collilineatus venoms and the pool of them. Moreover, the venom...
Tipo: Info:eu-repo/semantics/report Palavras-chave: Snake venoms; Crotalus durissus collilineatus; Antivenomic; Crotalic antivenom; Individual variation.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100601
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Cell migration inhibition activity of a non-RGD disintegrin from Crotalus durissus collilineatus venom J. Venom. Anim. Toxins incl. Trop. Dis.
Oliveira,Isadora Sousa de; Manzini,Rafaella Varzoni; Ferreira,Isabela Gobbo; Cardoso,Iara Aimê; Bordon,Karla de Castro Figueiredo; Machado,Ana Rita Thomazela; Antunes,Lusânia Maria Greggi; Rosa,José Cesar; Arantes,Eliane Candiani.
Abstract Background: In recent decades, snake venom disintegrins have received special attention due to their potential use in anticancer therapy. Disintegrins are small and cysteine-rich proteins present in snake venoms and can interact with specific integrins to inhibit their activities in cell-cell and cell-ECM interactions. These molecules, known to inhibit platelet aggregation, are also capable of interacting with certain cancer-related integrins, and may interfere in important processes involved in carcinogenesis. Therefore, disintegrin from Crotalus durissus collilineatus venom was isolated, structurally characterized and evaluated for its toxicity and ability to interfere with cell proliferation and migration in MDA-MB-231, a human breast cancer...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Crotalus durissus collilineatus; Non-RGD disintegrin; Cell migration; Cell adhesion; Human breast cancer; MDA-MB-231.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100319
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cDNA and deduced primary structure of basic phospholipase A2 with neurotoxic activity from the venom secretion of the Crotalus durissus collilineatus rattlesnake BJMBR
Fagundes,F.H.R.; Oliveira,M.; Huancahuire-Vega,S.; Romero-Vargas,F.F.; Ponce-Soto,L.A.; Marangoni,S..
To illustrate the construction of precursor complementary DNAs, we isolated mRNAs from whole venom samples. After reverse transcription polymerase chain reaction (RT-PCR), we amplified the cDNA coding for a neurotoxic protein, phospholipase A2 D49 (PLA2 D49), from the venom of Crotalus durissus collilineatus (Cdc PLA2). The cDNA encoding Cdc PLA2 from whole venom was sequenced. The deduced amino acid sequence of this cDNA has high overall sequence identity with the group II PLA2 protein family. Cdc PLA2 has 14 cysteine residues capable of forming seven disulfide bonds that characterize this group of PLA2 enzymes. Cdc PLA2 was isolated using conventional Sephadex G75 column chromatography and reverse-phase high performance liquid chromatography (RP-HPLC)....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Cdc PLA2; CDNA; Chick biventer cervicis; Crotalus durissus collilineatus; Mass spectrometry MALDI-TOF; Neurotoxic agents.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2010000300007
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