The malate synthase of Paracoccidioides brasiliensis is a linked surface protein that behaves as an anchorless adhesin

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dc.contributor.authorda Silva Neto, Benedito Rodrigues
dc.contributor.authorda Silva, Julhiany de Fatima [UNESP]
dc.contributor.authorMendes-Giannini, Maria José Soares [UNESP]
dc.contributor.authorLenzi, Henrique Leonel
dc.contributor.authorde Almeida Soares, Celia Maria
dc.contributor.authorPereira, Maristela
dc.contributor.institutionUniversidade Federal de Goiás (UFG)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionFiocruz MS
dc.date.accessioned2014-05-20T13:23:50Z
dc.date.available2014-05-20T13:23:50Z
dc.date.issued2009-12-24
dc.description.abstractBackground: The pathogenic fungus Paracoccidioides brasiliensis is the agent of paracoccidioidomycosis (PCM). This is a pulmonary mycosis acquired by inhalation of fungal airborne propagules that can disseminate to several organs and tissues leading to a severe form of the disease. Adhesion and invasion to host cells are essential steps involved in the internalization and dissemination of pathogens. Inside the host, P. brasiliensis may use the glyoxylate cycle for intracellular survival.Results: Here, we provide evidence that the malate synthase of P. brasiliensis (PbMLS) is located on the fungal cell surface, and is secreted. PbMLS was overexpressed in Escherichia coli, and polyclonal antibody was obtained against this protein. By using Confocal Laser Scanning Microscopy, PbMLS was detected in the cytoplasm and in the cell wall of the mother, but mainly of budding cells of the P. brasiliensis yeast phase. PbMLSr and its respective polyclonal antibody produced against this protein inhibited the interaction of P. brasiliensis with in vitro cultured epithelial cells A549.Conclusion: These observations indicated that cell wall-associated PbMLS could be mediating the binding of fungal cells to the host, thus contributing to the adhesion of fungus to host tissues and to the dissemination of infection, behaving as an anchorless adhesin.en
dc.description.affiliationUniv Fed Goias, Inst Ciencias Biol, Dept Bioquim & Biol Mol, Mol Biol Lab, BR-74001970 Goiania, Go, Brazil
dc.description.affiliationUNESP, Univ Estadual Paulista, Lab Micol Clin, Araraquara, SP, Brazil
dc.description.affiliationFiocruz MS, Inst Oswaldo Cruz, Lab Patol, BR-21045900 Rio de Janeiro, Brazil
dc.description.affiliationUnespUNESP, Univ Estadual Paulista, Lab Micol Clin, Araraquara, SP, Brazil
dc.description.sponsorshipMinisterio de Ciência e Tecnologia (MCT)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFinanciadora de Estudos e Projetos (FINEP)
dc.description.sponsorshipInternational Foundation for Science (IFS), Stockholm, Sweden
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.format.extent12
dc.identifierhttp://dx.doi.org/10.1186/1471-2180-9-272
dc.identifier.citationBmc Microbiology. London: Biomed Central Ltd., v. 9, p. 12, 2009.
dc.identifier.doi10.1186/1471-2180-9-272
dc.identifier.fileWOS000273911100001.pdf
dc.identifier.issn1471-2180
dc.identifier.orcid0000-0002-8059-0826
dc.identifier.urihttp://hdl.handle.net/11449/7252
dc.identifier.wosWOS:000273911100001
dc.language.isoeng
dc.publisherBiomed Central Ltd.
dc.relation.ispartofBMC Microbiology
dc.relation.ispartofjcr2.829
dc.relation.ispartofsjr1,242
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.titleThe malate synthase of Paracoccidioides brasiliensis is a linked surface protein that behaves as an anchorless adhesinen
dc.typeArtigo
dcterms.licensehttp://www.biomedcentral.com/about/license
dcterms.rightsHolderBiomed Central Ltd.
unesp.author.orcid0000-0002-8059-0826[3]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt
unesp.departmentAnálises Clínicas - FCFpt

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Araraquara - FCF - Faculdade de Ciências Farmacêuticas