31 research outputs found
Sightings of Pontoporia blainvillei (Gervais & D' Orbigny, 1844) and Sotalia fluviatilis (Gervais, 1853) (Cetacea) in South-eastern Brazil
Maternal Attachment and Children’s Quality of Life: The Mediating Role of Self-compassion and Parenting Stress
Nas teias da “rede de proteção”: internação compulsória de crianças e adolescentes e a judicialização da vida
Explaining parent-child (dis)agreement in generic and short stature-specific health-related quality of life reports: do family and social relationships matter?
Regional differences in clinical care among patients with type 1 diabetes in Brazil: Brazilian Type 1 Diabetes Study Group
Host plants of Lycaenidae on inflorescences in the central Brazilian cerrado
Volume: 44Start Page: 95End Page: 10
Purification and biochemical characterization of three myotoxins from bothrops mattogrossensis snake venom with toxicity against leishmania and tumor cells
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Previous issue date: 2014Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Núcleo de Saúde. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Núcleo de Saúde. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Núcleo de Saúde. Universidade Federal de Rondônia. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Núcleo de Saúde. Universidade Federal de Rondônia. Porto Velho, RO, Brazil. / Fundação Oswaldo Cruz. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Porto Velho, RO, Brazil.Universidade Federal Fluminense. Instituto de Biologia. Departamento de Biologia Celular e Molecular. Niterói, RJ, Brazil.Universidade Federal Fluminense. Instituto de Biologia. Departamento de Biologia Celular e Molecular. Niterói, RJ, Brazil.Universidade de São Paulo. Faculdade de Ciências Farmacêuticas. Ribeirão Preto, SP, Brazil.Universidade Federal de São João del Rei. Ouro Branco, MG, Brazil.Fundação Oswaldo Cruz. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Núcleo de Saúde. Universidade Federal de Rondônia. Porto Velho, RO, Brazil. / Fundação Oswaldo Cruz. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Núcleo de Saúde. Universidade Federal de Rondônia. Porto Velho, RO, Brazil. / Fundação Oswaldo Cruz. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Núcleo de Saúde. Universidade Federal de Rondônia. Porto Velho, RO, Brazil. / Fundação Oswaldo Cruz. Porto Velho, RO, Brazil.Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas Aplicadas à Saúde. Departamento de Medicina. Núcleo de Saúde. Universidade Federal de Rondônia. Porto Velho, RO, Brazil. / Fundação Oswaldo Cruz. Porto Velho, RO, Brazil.Bothrops mattogrossensis snake is widely distributed throughout eastern South America and is responsible for snakebites in this region. This paper reports the purification and biochemical characterization of three new phospholipases A2 (PLA2s), one of
which is presumably an enzymatically active Asp49 and two are very likely enzymatically inactive Lys49 PLA2 homologues. The purification was obtained after two chromatographic steps on ion exchange and reverse phase column. The 2D SDS-PAGE analysis revealed that the proteins have pI values around 10, are each made of a single chain, and have molecular masses near 13 kDa, which was confirmed by MALDI-TOF mass spectrometry. The N-terminal similarity analysis of the sequences showed that the proteins are highly homologous with other Lys49 and Asp49 PLA2s from Bothrops species. The PLA2s isolated were named BmatTX-I (Lys49 PLA2-like), BmatTX-II (Lys49 PLA2-like), and BmatTX-III (Asp49 PLA2). The PLA2s induced cytokine release frommouse neutrophils and showed cytotoxicity towards JURKAT (leukemia T) and SK-BR-3 (breast adenocarcinoma) cell
lines and promastigote forms of Leishmania amazonensis. The structural and functional elucidation of snake venoms components may contribute to a better understanding of the mechanism of action of these proteins during envenomation and their potential
pharmacological and therapeutic applications
Removal of N-Terminal Peptide Impacts Structural Aspects of an IgE-Reactive Recombinant Der p 5
(1) Background: Modification of the structural elements of allergens is widely used in the field of allergies. The goal of the present research was to express, purify, and characterize the shortened recombinant group 5 allergen of Dermatophagoides pteronyssinus (rDer p 5). (2) Methods: rDer p 5 storage stability and aggregation capacity were explored through in silico analysis, dynamic light scattering (DLS), and SDS-PAGE. Serum IgE reactivity and cytokine amount were investigated in sera or cell culture supernatants through ELISA, MULTIPLEX®, and Western blot analysis using sera from sensitized humans from Brazil, Colombia, and Ecuador. (3) Results: Dimeric rDer p 5 was detected through native PAGE, and this result was confirmed by data from DLS. The protein was thermically stable, as it did not degrade at 4 °C for 21 days. The shortened rDer p 5 was classified as a major IgE allergen in Brazil and Colombia, but minor in Ecuador. IL-13, IL-10, IL-1β, and IL-6 were significantly elevated in the sera of rDer p 5-reactive patients. The same cytokines plus IL-5 were more secreted by human cells upon rDer p 5 stimulation. (4) Conclusions: N-terminal peptide deletion led to a higher rDer p 5 folding stability, which, even though dimeric, was an IgE-reactive protein. Therefore, rDer p 5 could be used for molecular diagnostic applications or as backbone for hypoallergen design