Intermolecular interactions of the malate synthase of Paracoccidioides spp

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dc.creatorOliveira, Karine Martins de
dc.creatorSilva Neto, Benedito Rodrigues da
dc.creatorRocha, Juliana Alves Parente
dc.creatorSilva, Roosevelt Alves da
dc.creatorQuintino, Guilherme Oliveira
dc.creatorVoltan, Aline Raquel
dc.creatorGiannini, Maria José Soares Mendes
dc.creatorSoares, Célia Maria de Almeida
dc.creatorPereira, Maristela
dc.date.accessioned2018-07-11T13:59:34Z
dc.date.available2018-07-11T13:59:34Z
dc.date.issued2013
dc.description.abstractBackground: The fungus Paracoccidioides spp is the agent of paracoccidioidomycosis (PCM), a pulmonary mycosis acquired by the inhalation of fungal propagules. Paracoccidioides malate synthase (PbMLS) is important in the infectious process of Paracoccidioides spp because the transcript is up-regulated during the transition from mycelium to yeast and in yeast cells during phagocytosis by murine macrophages. In addition, PbMLS acts as an adhesin in Paracoccidioides spp. The evidence for the multifunctionality of PbMLS indicates that it could interact with other proteins from the fungus and host. The objective of this study was to identify and analyze proteins that possibly bind to PbMLS (PbMLS-interacting proteins) because protein interactions are intrinsic to cell processes, and it might be possible to infer the function of a protein through the identification of its ligands. Results: The search for interactions was performed using an in vivo assay with a two-hybrid library constructed in S. cerevisiae; the transcripts were sequenced and identified. In addition, an in vitro assay using pull-down GST methodology with different protein extracts (yeast, mycelium, yeast-secreted proteins and macrophage) was performed, and the resulting interactions were identified by mass spectrometry (MS). Some of the protein interactions were confirmed by Far-Western blotting using specific antibodies, and the interaction of PbMLS with macrophages was validated by indirect immunofluorescence and confocal microscopy. In silico analysis using molecular modeling, dynamics and docking identified the amino acids that were involved in the interactions between PbMLS and PbMLS-interacting proteins. Finally, the interactions were visualized graphically using Osprey software. Conclusion: These observations indicate that PbMLS interacts with proteins that are in different functional categories, such as cellular transport, protein biosynthesis, modification and degradation of proteins and signal transduction. These data suggest that PbMLS could play different roles in the fungal cell.pt_BR
dc.identifier.citationOLIVEIRA, Karine Martins de; SILVA Neto, Benedito Rodrigues da; PARENTE, Juliana Alves; SILVA, Roosevelt Alves da; QUINTINO, Guilherme Oliveira; VOLTAN, Aline Raque; MENDES-GIANNINI, Maria José Soares; SOARES, Célia Maria de Almeida; PEREIRA, Maristela. Intermolecular interactions of the malate synthase of Paracoccidioides spp. BMC Microbiology, London, v. 13, n. 107, p. 1-14, 2013.pt_BR
dc.identifier.doi10.1186/1471-2180-13-107
dc.identifier.issne- 1471-2180
dc.identifier.urihttp://repositorio.bc.ufg.br/handle/ri/15378
dc.language.isoengpt_BR
dc.publisher.countryGra-bretanhapt_BR
dc.publisher.departmentInstituto de Ciências Biológicas - ICB (RG)pt_BR
dc.rightsAcesso Abertopt_BR
dc.subjectParacoccidioides spppt_BR
dc.subjectProtein-protein interactionspt_BR
dc.subjectMalate synthasept_BR
dc.titleIntermolecular interactions of the malate synthase of Paracoccidioides spppt_BR
dc.typeArtigopt_BR

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