A new Paracoccidioides brasiliensis 70-kDa heat shock protein reacts with sera from paracoccidioidomycosis patients

A new Paracoccidioides brasiliensis 70-kDa heat shock protein reacts with sera from paracoccidioidomycosis patients

Autor Bisio, L. C. Google Scholar
Silva, S. P. Google Scholar
Pereira, I. S. Google Scholar
Xavier, MAS Google Scholar
Venancio, E. J. Google Scholar
Puccia, R. Google Scholar
Soares, CMA Google Scholar
Felipe, MSS Google Scholar
Instituição Universidade de Brasília (UnB)
Universidade Federal de Goiás (UFG)
Universidade Federal de São Paulo (UNIFESP)
Universidade Estadual de Londrina (UEL)
Novo Nordisk Prod Farmaceut Brasil
Resumo A cDNA coding for a new member of the 70-kDa heat shock proteins (HSP70) family from the dimorphic and pathogenic fungus, Paracoccidioides brasiliensis, was cloned and characterized. the cDNA-deduced sequence coded for 655 amino acid residues and showed 95% identity to a previously described P. brasiliensis hsp70 gene. Cytoplasmic and typical nuclear localization signals, which indicate induction upon stress, were identified in the deduced peptide. the complete hsp70 cDNA coding region was cloned into a pGEX 4T-3 plasmid and expressed in Escherichia coli as a glutathione-S-transferase-tagged fusion protein. the recombinant protein reacted with a rabbit polyclonal antibody against HSP70. Western immunoblot experiments demonstrated that sera from paracoccidioidomycosis patients recognized the purified recombinant protein, suggesting an immunological role for this protein in the infectious process. the antigenicity analysis of rHSP70 detected three internal peptides that could act as activators of T-cell proliferation.
Palavra-chave antigenic peptides
Paracoccidioides brasiliensis
protein expression
Idioma Inglês
Data de publicação 2005-09-01
Publicado em Medical Mycology. Abingdon: Taylor & Francis Ltd, v. 43, n. 6, p. 495-503, 2005.
ISSN 1369-3786 (Sherpa/Romeo, fator de impacto)
Publicador Taylor & Francis Ltd
Extensão 495-503
Fonte http://dx.doi.org/10.1080/13693780400029478
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000233320300003
Endereço permanente http://repositorio.unifesp.br/handle/11600/28456

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