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Escolher formato: Padrão Ficha Formato Reduzido Nomes MARC Campos MARC
No. Registro   002711846
Tipo de material   ARTIGO DE PERIODICO - INTERNACIONAL
Cód. publicação   Link10.1128/IAI.02074-14 DOI
Entrada Principal   LinkBatista, Milene Tavares (*)
Título   LinkImmunogenicity and in vitro and in vivo protective effects of antibodies targeting a recombinant form of the Streptococcus mutans P1 surface protein.
Imprenta   Washington, 2014.
Descrição   p. 4978-4988.
Idioma   Inglês
Nota Local   Fator de impacto: 3.731
Assunto   LinkMICROBIOLOGIA
  LinkSTREPTOCOCCUS MUTANS
  LinkANTICORPOS
  LinkRECOMBINAÇÃO GENÉTICA
Autor Secundário   LinkSouza, Renata D. (*) Universidade de São Paulo, Instituto de Ciências Biomédicas, Departamento de Microbiologia, São Paulo, Brasil NAC
  LinkFerreira, Ewerton Lucena (*) Universidade de São Paulo, Instituto de Ciências Biomédicas, Departamento de Microbiologia, São Paulo, Brasil NAC
  LinkRobinette, Rebekah (*) University of Florida, College of Dentistry, Department of Oral Biology INT
  LinkCrowley, Paula J. (*) University of Florida, College of Dentistry, Department of Oral Biology INT
  LinkRodrigues, Juliana F. (*)
  LinkBrady, L. Jeannine (*) University of Florida, College of Dentistry, Department of Oral Biology INT
  LinkFerreira, Luis Carlos de Souza
  LinkFerreira, Rita de Cássia Café
Fonte   LinkIn: Infection and Immunit, Washington, v. 82, n. 12, p. 4978-4988, 2014, ISSN: 1098-5522
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Resumo/Outros   Streptococcus mutans is a major etiologic agent of dental caries, a prevalent worldwide infectious disease and a serious public health concern. The surface-localized S. mutans P1 adhesin contributes to tooth colonization and caries formation. P1 is a large (185-kDa) and complex multidomain protein considered a promising target antigen for anticaries vaccines. Previous observations showed that a recombinant P1 fragment (P1(39-512)), produced in Bacillus subtilis and encompassing a functional domain, induces antibodies that recognize the native protein and interfere with S. mutans adhesion in vitro. In the present study, we further investigated the immunological features of P1(39-512) in combination with the following different adjuvants after parenteral administration to mice: alum, a derivative of the heat-labile toxin (LT), and the phase 1 flagellin of S. Typhimurium LT2 (FliCi). Our results demonstrated that recombinant P1(39-512) preserves relevant conformational epitopes as well as salivary agglutinin (SAG)-binding activity. Coadministration of adjuvants enhanced anti-P1 serum antibody responses and affected both epitope specificity and immunoglobulin subclass switching. Importantly, P1(39-512)-specific antibodies raised in mice immunized with adjuvants showed significantly increased inhibition of S. mutans adhesion to SAG, with less of an effect on SAG-mediated bacterial aggregation, an innate defense mechanism. Oral colonization of mice by S. mutans was impaired in the presence of anti-P1(39-512) antibodies, particularly those raised in combination with adjuvants. In conclusion, our results confirm the utility of P1(39-512) as a potential candidate for the development of anticaries vaccines and as a tool for functional studies of S. mutans P1
 
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Itens na Biblioteca   ICB-Inst. Ciências BiomédicaLibrary Info
Unidade USP   ICB -- INSTITUTO DE CIÊNCIAS BIOMÉDICAS
  ICB -- INSTITUTO DE CIÊNCIAS BIOMÉDICAS

Escolher formato: Padrão Ficha Formato Reduzido Nomes MARC Campos MARC


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