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Pesquisa : D08.811.913.696.445.600 [Categoria DeCS]
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Id: biblio-990188
Autor: Ortiz-Joya, Lesly; Contreras-Rodríguez, Luis Ernesto; Ramírez-Hernández, María Helena.
Título: Protein-protein interactions of the nicotinamide/nicotinate mononucleotide adenylyltransferase of Leishmania braziliensis
Fonte: Mem. Inst. Oswaldo Cruz;114:e180506, 2019. tab, graf.
Idioma: en.
Projeto: Colciencias.
Resumo: BACKGROUND Nicotinamide adenine dinucleotide (NAD) plays a central role in energy metabolism and integrates cellular metabolism with signalling and gene expression. NAD biosynthesis depends on the enzyme nicotinamide/nicotinate mononucleotide adenylyltransferase (NMNAT; EC: 2.7.7.1/18), in which converge the de novo and salvage pathways. OBJECTIVE The purpose of this study was to analyse the protein-protein interactions (PPI) of NMNAT of Leishmania braziliensis (LbNMNAT) in promastigotes. METHODS Transgenic lines of L. braziliensis promastigotes were established by transfection with the pSP72αneoαLbNMNAT-GFP vector. Soluble protein extracts were prepared, co-immunoprecipitation assays were performed, and the co-immunoprecipitates were analysed by mass spectrometry. Furthermore, bioinformatics tools such as network analysis were applied to generate a PPI network. FINDINGS Proteins involved in protein folding, redox homeostasis, and translation were found to interact with the LbNMNAT protein. The PPI network indicated enzymes of the nicotinate and nicotinamide metabolic routes, as well as RNA-binding proteins, the latter being the point of convergence between our experimental and computational results. MAIN CONCLUSION We constructed a model of PPI of LbNMNAT and showed its association with proteins involved in various functions such as protein folding, redox homeostasis, translation, and NAD synthesis.
Descritores: Leishmania braziliensis
Mapas de Interação de Proteínas
-NAD/análise
Nicotinamida-Nucleotídeo Adenililtransferase
Responsável: BR1.1 - BIREME


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Id: biblio-955126
Autor: Contreras-Rodríguez, Luis Ernesto; Marin-Mogollon, Catherin Yizet; Sánchez-Mejía, Lina Marcela; Ramírez-Hernández, María Helena.
Título: Structural insights into Plasmodium falciparum nicotinamide mononucleotide adenylyltransferase: oligomeric assembly
Fonte: Mem. Inst. Oswaldo Cruz;113(9):e180073, 2018. tab, graf.
Idioma: en.
Resumo: The biochemical pathways involved in nicotinamide adenine dinucleotide (NAD) biosynthesis converge at the enzymatic step catalysed by nicotinamide mononucleotide adenylyltransferase (NMNAT, EC: 2.7.7.1). The majority of NMNATs are assembled into homo-oligomeric states that comprise 2-6 subunits. Recently, the NMNAT of Plasmodium falciparum (PfNMNAT) has been identified as a pharmacological target. The enzymatic characterisation, cellular location, and tertiary structure of the PfNMNAT protein have been reported. Nonetheless, its quaternary structure remains to be explored. The present study describes the oligomeric assembly of the 6 x His-PfNMNAT recombinant protein using immobilised metal affinity chromatography coupled with size exclusion chromatography (SEC) and native protein electrophoresis combined with Ferguson plot graphing. These chromatographic approaches resulted in the elution of an active monomer from the SEC column, whereas the Ferguson plot indicated a dimeric assembly of the 6 x His-PfNMNAT protein.
Descritores: Plasmodium falciparum/enzimologia
Plasmodium falciparum/química
-Cromatografia de Afinidade
Nicotinamida-Nucleotídeo Adenililtransferase
Nicotinamida-Nucleotídeo Adenililtransferase/uso terapêutico
Limites: Seres Humanos
Responsável: BR1.1 - BIREME


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Id: biblio-829246
Autor: Sánchez-Lancheros, Diana Milena; Ospina-Giraldo, Luis Fernando; Ramírez-Hernández, María Helena.
Título: Nicotinamide mononucleotide adenylyltransferase of Trypanosoma cruzi (TcNMNAT): a cytosol protein target for serine kinases
Fonte: Mem. Inst. Oswaldo Cruz;111(11):670-675, Nov. 2016. graf.
Idioma: en.
Projeto: Universidad Nacional de Colombia; . Colciencias.
Resumo: Nicotinamide/nicotinate adenine dinucleotide (NAD+/NaAD) performs essential functions in cell metabolism and energy production due to its redox properties. The nicotinamide/nicotinate mononucleotide adenylyltransferase (NMNAT, EC 2.7.7.1/18) enzyme catalyses the key step in the biosynthesis of NAD+. Previously, the enzyme NMNAT was identified in Trypanosoma cruzi (TcNMNAT), a pathogenic agent with epidemiological importance in Latin America. To continue with the functional characterisation of this enzyme, its subcellular location and its possible post-translational modifications were examined in this study. For this, polyclonal antibodies were generated in mice, with soluble and denatured recombinant protein being used to detect the parasite’s NMNAT. Immunodetection assays were performed on whole extracts of T. cruzi, and an approximation of its intracellular location was determined using confocal microscopy on wild and transgenic parasites, which revealed the cytosol distribution patterns. This localisation occurs according to the needs of the dinucleotides that exist in this compartment. Additionally, a bioinformatics study was performed as a first approach to establish the post-translational modifications of the enzyme. Possible phosphorylation events were experimentally analysed by western blot, highlighting TcNMNAT as a potential target for serine kinases.
Descritores: Nicotinamida-Nucleotídeo Adenililtransferase/metabolismo
Proteínas de Protozoários/metabolismo
Trypanosoma cruzi/enzimologia
-Sequência de Aminoácidos
Citosol/parasitologia
Interações Hospedeiro-Parasita
Camundongos
Camundongos Endogâmicos BALB C
Nicotinamida-Nucleotídeo Adenililtransferase/isolamento & purificação
Fosforilação
Proteínas Serina-Treonina Quinases
Proteínas de Protozoários/isolamento & purificação
Limites: Animais
Responsável: BR1.1 - BIREME


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Id: lil-764585
Autor: Niño, Carlos H; Forero-Baena, Nicolás; Contreras, Luis E; Sánchez-Lancheros, Diana; Figarella, Katherine; Ramírez, María H.
Título: Identification of the nicotinamide mononucleotide adenylyltransferase of Trypanosoma cruzi
Fonte: Mem. Inst. Oswaldo Cruz;110(7):890-897, Nov. 2015. tab, graf.
Idioma: en.
Projeto: DIB-UNAL; . IDEA Foundation.
Resumo: The intracellular parasite Trypanosomacruzi is the aetiological agent of Chagas disease, a public health concern with an increasing incidence rate. This increase is due, among other reasons, to the parasite’s drug resistance mechanisms, which require nicotinamide adenine dinucleotide (NAD+). Furthermore, this molecule is involved in metabolic and intracellular signalling processes necessary for the survival of T. cruzithroughout its life cycle. NAD+biosynthesis is performed by de novo and salvage pathways, which converge on the step that is catalysed by the enzyme nicotinamide mononucleotide adenylyltransferase (NMNAT) (enzyme commission number: 2.7.7.1). The identification of the NMNAT of T. cruziis important for the development of future therapeutic strategies to treat Chagas disease. In this study, a hypothetical open reading frame (ORF) for NMNAT was identified in the genome of T. cruzi.The corresponding putative protein was analysed by simulating structural models. The ORF was amplified from genomic DNA by polymerase chain reaction and was further used for the construction of a corresponding recombinant expression vector. The expressed recombinant protein was partially purified and its activity was evaluated using enzymatic assays. These results comprise the first identification of an NMNAT in T. cruziusing bioinformatics and experimental tools and hence represent the first step to understanding NAD+ metabolism in these parasites.
Descritores: Nicotinamida-Nucleotídeo Adenililtransferase/metabolismo
Trypanosoma cruzi/enzimologia
-Sequência de Aminoácidos
Modelos Moleculares
Dados de Sequência Molecular
Nicotinamida-Nucleotídeo Adenililtransferase/genética
Alinhamento de Sequência
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME



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