skip to main content
Idioma:
Primo Advanced Search
Primo Advanced Search Query Term
Primo Advanced Search prefilters
Busca Simples

Antibodies to a 75-KDA protein from Paracoccidioides brasiliensis protect against experimental paracoccidioidomycosis

P Xander L S Feitosa; R A Mortara; Mário Mariano; J D Lopes; Meeting of the Brazilian Society for Immunology (31. 2006 Búzios)

Abstracts São Paulo, SP: Brazilian Society for Immunology, 2006

São Paulo 2006

Item não circula. Consulte sua biblioteca.(Acessar)

  • Título:
    Antibodies to a 75-KDA protein from Paracoccidioides brasiliensis protect against experimental paracoccidioidomycosis
  • Autor: P Xander
  • L S Feitosa; R A Mortara; Mário Mariano; J D Lopes; Meeting of the Brazilian Society for Immunology (31. 2006 Búzios)
  • Assuntos: IMUNOLOGIA
  • É parte de: Abstracts São Paulo, SP: Brazilian Society for Immunology, 2006
  • Notas: Disponível em CD-ROM
  • Descrição: Introduction and Objectives: Paracoccidioides brasiliensis is a dimorphic fungus that causes paracoccidioidomycosis (PCM), one of the most prevalent systemic mycosis in Latin America. The fungus presents a complex structure of proteins and glycoproteins whose molecular weight range from 13 to 148 kDa. The purpose of this study was the production and characterization of mAbs against a protein of 75-kDa of P. brasiliensis as well as to characterize the target antigen to study their possible protective capacity against experimental PCM in mice. Methods and Results: Mice were immunized with macerated polyacrilamide gel containing the protein of 75-kDa. Two hybridoma lines were generated: one IgM (1G6) and one IgG (5E7C) isotypes. Both mAbs bound to dividing yeast cells of P. brasiliensis and the addition of antibodies to the cultures clearly inhibited fungal growth. In vitro experiments showed that mAbs facilitate the phagocytosis and kill intracellular P. brasiliensis by peritoneal macrophages. Administration of mAbs by passive immunization assays reduced fungal burden and decrease pulmonary inflammation. The protein recognized by 5E7C mAb was cut off two-dimensional gels and one 16 amino acid peptide sequence was obtained. A BLAST search revealed homology of this sequence with hypothetical proteins of Magnaporthe grisea, Neurospora crassa, Gibberella zeae and Coccidioides imitis.. The hypothetical protein in Aspergillus fumigatus
    seems to have esterase activity. The antigen recognized by mAbs was purified from crude exoantigens of P. brasiliensis yeast cells and preliminary results showed that the protein recognized by mAbs probably contain a phosphomonoesterase activity. Conclusion: MAbs against a 75-kDa protein were protective in the murine experimental model of infection and the purified antigen probably contains acid phosphatase activity.
  • Editor: São Paulo
  • Data de criação/publicação: 2006
  • Formato: res. ID.049.
  • Idioma: Inglês
Links
Voltar para lista de resultados
Ir para página anteriorAnterior Resultado  5 AvançarIr para próxima página

  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

Buscando em bases de dados remotas. Favor aguardar.