No. Registro | 002711846 |
Tipo de material | ARTIGO DE PERIODICO - INTERNACIONAL |
Cód. publicação | 10.1128/IAI.02074-14 DOI |
Entrada Principal | Batista, Milene Tavares (*) |
Título | Immunogenicity 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 | MICROBIOLOGIA |
| STREPTOCOCCUS MUTANS |
| ANTICORPOS |
| RECOMBINAÇÃO GENÉTICA |
Autor Secundário | Souza, Renata D. (*) Universidade de São Paulo, Instituto de Ciências Biomédicas, Departamento de Microbiologia, São Paulo, Brasil NAC |
| Ferreira, Ewerton Lucena (*) Universidade de São Paulo, Instituto de Ciências Biomédicas, Departamento de Microbiologia, São Paulo, Brasil NAC |
| Robinette, Rebekah (*) University of Florida, College of Dentistry, Department of Oral Biology INT |
| Crowley, Paula J. (*) University of Florida, College of Dentistry, Department of Oral Biology INT |
| Rodrigues, Juliana F. (*) |
| Brady, L. Jeannine (*) University of Florida, College of Dentistry, Department of Oral Biology INT |
| Ferreira, Luis Carlos de Souza |
| Ferreira, Rita de Cássia Café |
Fonte | In: Infection and Immunit, Washington, v. 82, n. 12, p. 4978-4988, 2014, ISSN: 1098-5522 |
Localiz.Eletrônica |
"Clicar" sobre o botão para acesso ao texto completo |
|
"Clicar" sobre o botão para acesso ao Currículo Lattes de Luis Carlos de Souza Ferreira |
|
"Clicar" sobre o botão para acesso ao Currículo Lattes de Rita de Cássia Café Ferreira |
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 |
| |
Acervo Geral | Todos os itens |
Itens na Biblioteca | ICB-Inst. Ciências Biomédica |
Unidade USP | ICB -- INSTITUTO DE CIÊNCIAS BIOMÉDICAS |
| ICB -- INSTITUTO DE CIÊNCIAS BIOMÉDICAS |