Paracoccidoides brasiliensis 30 kDa Adhesin: Identification as a 14-3-3 Protein, Cloning and Subcellular Localization in Infection Models

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dc.contributor.authorSilva, Julhiany de Fatima da [UNESP]
dc.contributor.authorOliveira, Haroldo César de [UNESP]
dc.contributor.authorMarcos, Caroline Maria [UNESP]
dc.contributor.authorSilva, Rosângela Aparecida Moraes da [UNESP]
dc.contributor.authorCosta, Tania Alves da
dc.contributor.authorCalich, Vera Lucia García
dc.contributor.authorAlmeida, Ana Marisa Fusco [UNESP]
dc.contributor.authorMendes-Giannini, Maria José Soares [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-27T11:29:00Z
dc.date.available2014-05-27T11:29:00Z
dc.date.issued2013-04-30
dc.description.abstractParacoccidoides brasiliensis adhesion to lung epithelial cells is considered an essential event for the establishment of infection and different proteins participate in this process. One of these proteins is a 30 kDa adhesin, pI 4.9 that was described as a laminin ligand in previous studies, and it was more highly expressed in more virulent P. brasiliensis isolates. This protein may contribute to the virulence of this important fungal pathogen. Using Edman degradation and mass spectrometry analysis, this 30 kDa adhesin was identified as a 14-3-3 protein. These proteins are a conserved group of small acidic proteins involved in a variety of processes in eukaryotic organisms. However, the exact function of these proteins in some processes remains unknown. Thus, the goal of the present study was to characterize the role of this protein during the interaction between the fungus and its host. To achieve this goal, we cloned, expressed the 14-3-3 protein in a heterologous system and determined its subcellular localization in in vitro and in vivo infection models. Immunocytochemical analysis revealed the ubiquitous distribution of this protein in the yeast form of P. brasiliensis, with some concentration in the cytoplasm. Additionally, this 14-3-3 protein was also present in P. brasiliensis cells at the sites of infection in C57BL/6 mice intratracheally infected with P. brasiliensis yeast cells for 72 h (acute infections) and 30 days (chronic infection). An apparent increase in the levels of the 14-3-3 protein in the cell wall of the fungus was also noted during the interaction between P. brasiliensis and A549 cells, suggesting that this protein may be involved in host-parasite interactions, since inhibition assays with the protein and this antibody decreased P. brasiliensis adhesion to A549 epithelial cells. Our data may lead to a better understanding of P. brasiliensis interactions with host tissues and paracoccidioidomycosis pathogenesis. © 2013 Silva et al.en
dc.description.affiliationDepartment of Clinical Analyses Faculty of Pharmaceutical Sciences São Paulo State University - University Estadual Paulista Araraquara, São Paulo
dc.description.affiliationDepartment of Immunology Biomedical Institute São Paulo University, São Paulo
dc.description.affiliationUnespDepartment of Clinical Analyses Faculty of Pharmaceutical Sciences São Paulo State University - University Estadual Paulista Araraquara, São Paulo
dc.identifierhttp://dx.doi.org/10.1371/journal.pone.0062533
dc.identifier.citationPLoS ONE, v. 8, n. 4, 2013.
dc.identifier.doi10.1371/journal.pone.0062533
dc.identifier.file2-s2.0-84876989266.pdf
dc.identifier.issn1932-6203
dc.identifier.orcid0000-0002-8059-0826
dc.identifier.scopus2-s2.0-84876989266
dc.identifier.urihttp://hdl.handle.net/11449/75190
dc.identifier.wosWOS:000319077300073
dc.language.isoeng
dc.relation.ispartofPLOS ONE
dc.relation.ispartofjcr2.766
dc.relation.ispartofsjr1,164
dc.rights.accessRightsAcesso aberto
dc.sourceScopus
dc.subjectadhesin
dc.subjectprotein 14 3 3
dc.subjectanimal experiment
dc.subjectanimal model
dc.subjectanimal tissue
dc.subjectantibody production
dc.subjectcell adhesion
dc.subjectcellular distribution
dc.subjectcolony forming unit
dc.subjectcontrolled study
dc.subjectdisease model
dc.subjectfungal cell wall
dc.subjectfungus
dc.subjectgene sequence
dc.subjectheterologous expression
dc.subjecthost pathogen interaction
dc.subjectimmunocytochemistry
dc.subjectin vitro study
dc.subjectin vivo study
dc.subjectmass spectrometry
dc.subjectmolecular cloning
dc.subjectmouse
dc.subjectmycosis
dc.subjectnonhuman
dc.subjectnucleotide sequence
dc.subjectParacoccidoides brasiliensis
dc.subjectpathogenesis
dc.subjectprotein determination
dc.subjectprotein function
dc.subjectprotein localization
dc.subjectprotein purification
dc.subjectsequence homology
dc.subjectSouth American blastomycosis
dc.titleParacoccidoides brasiliensis 30 kDa Adhesin: Identification as a 14-3-3 Protein, Cloning and Subcellular Localization in Infection Modelsen
dc.typeArtigo
dcterms.licensehttp://www.plos.org/open-access/
unesp.author.lattes3716273524139678[7]
unesp.author.orcid0000-0002-8059-0826[8]
unesp.author.orcid0000-0002-2115-8988[7]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt

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