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dc.contributor.authorMariutti, Ricardo B. [UNESP]
dc.contributor.authorSouza, Tatiana A. C. B.
dc.contributor.authorUllah, Anwar [UNESP]
dc.contributor.authorCaruso, Icaro P. [UNESP]
dc.contributor.authorMoraes, Fábio R. de [UNESP]
dc.contributor.authorZanphorlin, Leticia M.
dc.contributor.authorTartaglia, Natayme R.
dc.contributor.authorSeyffert, Nubia
dc.contributor.authorAzevedo, Vasco A.
dc.contributor.authorLe Loir, Yves
dc.contributor.authorMurakami, Mário T.
dc.contributor.authorArni, Raghuvir K. [UNESP]
dc.date.accessioned2015-12-07T15:40:37Z
dc.date.available2015-12-07T15:40:37Z
dc.date.issued2015-11-06
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2015.08.083
dc.identifier.citationBiochemical And Biophysical Research Communications, v. 467, n. 1, p. 171-117, 2015.
dc.identifier.issn1090-2104
dc.identifier.urihttp://hdl.handle.net/11449/131689
dc.description.abstractExfoliative toxins are serine proteases secreted by Staphylococcus aureus that are associated with toxin-mediated staphylococcal syndromes. To date, four different serotypes of exfoliative toxins have been identified and 3 of them (ETA, ETB, and ETD) are linked to human infection. Among these toxins, only the ETD structure remained unknown, limiting our understanding of the structural determinants for the functional differentiation between these toxins. We recently identified an ETD-like protein associated to S. aureus strains involved in mild mastitis in sheep. The crystal structure of this ETD-like protein was determined at 1.95 Å resolution and the structural analysis provide insights into the oligomerization, stability and specificity and enabled a comprehensive structural comparison with ETA and ETB. Despite the highly conserved molecular architecture, significant differences in the composition of the loops and in both the N- and C-terminal α-helices seem to define ETD-like specificity. Molecular dynamics simulations indicate that these regions defining ET specificity present different degrees of flexibility and may undergo conformational changes upon substrate recognition and binding. DLS and AUC experiments indicated that the ETD-like is monomeric in solution whereas it is present as a dimer in the asymmetric unit indicating that oligomerization is not related to functional differentiation among these toxins. Differential scanning calorimetry and circular dichroism assays demonstrated an endothermic transition centered at 52 °C, and an exothermic aggregation in temperatures up to 64 °C. All these together provide insights about the mode of action of a toxin often secreted in syndromes that are not associated with either ETA or ETB.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científco e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.format.extent171-177
dc.language.isoeng
dc.publisherElsevier B. V.
dc.relation.ispartofBiochemical And Biophysical Research Communications
dc.sourcePubMed
dc.subjectCrystal structureen
dc.subjectExfoliative toxin d-like proteinen
dc.subjectStaphylococcus aureusen
dc.subjectToxin-mediated staphylococcal syndromesen
dc.titleCrystal structure of Staphylococcus aureus exfoliative toxin D-like protein: structural basis for the high specificity of exfoliative toxinsen
dc.typeArtigo
dcterms.rightsHolderElsevier B. V.
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionInstituto Carlos Chagas (ICC)
dc.contributor.institutionLaboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE)
dc.contributor.institutionUniversidade Federal de Minas Gerais (UFMG)
dc.contributor.institutionFrench National Institute for Agricultural Research (INRA)
dc.contributor.institutionAgrocampus Ouest
dc.contributor.institutionLaboratório Nacional de Biociências (LNBio)
dc.description.affiliationMulti User Center for Biomolecular Innovation, Department of Physics, IBILCE/UNESP, São José do Rio Preto, SP, Brazil.
dc.description.affiliationCarlos Chagas Institute, FIOCRUZ-PR, Curitiba, PR, Brazil.
dc.description.affiliationBioethanol Science and Technology Laboratory (CTBE), National Center for Research in Energy and Materials, Campinas, SP, 13083-970, Brazil.
dc.description.affiliationCellular and Molecular Genetics Laboratory, Institute of Biological Sciences, Federal University of Minas Gerais, Belo Horizonte, MG, 270-901, Brazil; INRA, UMR1253 STLO, Science et Technologie du Lait et de l'œuf, F-35042 Rennes, France; Agrocampus Ouest, UMR1253 STLO, F-35042 Rennes, France.
dc.description.affiliationCellular and Molecular Genetics Laboratory, Institute of Biological Sciences, Federal University of Minas Gerais, Belo Horizonte, MG, 270-901, Brazil.
dc.description.affiliationINRA, UMR1253 STLO, Science et Technologie du Lait et de l'œuf, F-35042 Rennes, France; Agrocampus Ouest, UMR1253 STLO, F-35042 Rennes, France.
dc.description.affiliationBrazilian Biosciences National Laboratory (LNBio), National Center for Research in Energy and Materials, Campinas, SP, 13083-970, Brazil.
dc.description.affiliationMulti User Center for Biomolecular Innovation, Department of Physics, IBILCE/UNESP, São José do Rio Preto, SP, Brazil.
dc.description.affiliationUnespMulti User Center for Biomolecular Innovation, Department of Physics, IBILCE/UNESP, São José do Rio Preto, SP, Brazil.
dc.identifier.doi10.1016/j.bbrc.2015.08.083
dc.rights.accessRightsAcesso restrito
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt
dc.identifier.pubmed26299923
dc.relation.ispartofsjr1,087
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