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The possible role of the activity of mycobacterium leprae hsp65 on the experimental autoimmune uveitis [EAU]

E. B. Marengo F. C. V Portaro; A. G Commodaro; L. D. V Moraes; M. A Hayashi; D. C Pimenta; Beatriz Lieblich Fernandes; Luiz Vicente Rizzo; T Yamane; Antonio Carlos Martins de Camargo; O. A Sant'Anna; Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq (33. 2004 Caxambu)

Programa e resumos Caxambu, MG

Caxambu 2004

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  • Título:
    The possible role of the activity of mycobacterium leprae hsp65 on the experimental autoimmune uveitis [EAU]
  • Autor: E. B. Marengo
  • F. C. V Portaro; A. G Commodaro; L. D. V Moraes; M. A Hayashi; D. C Pimenta; Beatriz Lieblich Fernandes; Luiz Vicente Rizzo; T Yamane; Antonio Carlos Martins de Camargo; O. A Sant'Anna; Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq (33. 2004 Caxambu)
  • Assuntos: IMUNOLOGIA; MICROBIOLOGIA
  • É parte de: Programa e resumos Caxambu, MG
  • Notas Locais: Disponível somente em CD-ROM
  • Descrição: Heat shock proteins of the hsp60 family are molecular chaperones that guide several steps during synthesis, transport and degradation of proteins. They are abundant in prokaryotic and eukaryotic cells and highly conserved during evolution. Both the microbial and the mammalian hsp60 belong to an important protein family that are major targets for the immune defense against infection. On the other hand, the microbial hsp60 have been implicated in autoimmune diseases, such as chronic inammation and atherosclerosis. The amino acid sequence alignment of M. leprae hsp65 (chaperonin 2) with the E. coli HslVU protease suggested two putative threonine catalytic groups, one in the Ndomain (Thr136-Lys168-Tyr264) and the other in the C-domain (Thr375-Lys409-Ser502); mutagenesis studies showed that the amino acid residues Thr375-Lys409-Ser502 at the C-domain form the catalytic group carries out the main proteolytic activity of the M. leprae hsp65. In the present study, it was compared the amino acid sequences of several hsps belonging to the hsp60 family, mainly the M. leprae hsp65. The possible pathophysiological implication of the proteolytic activity of the M. leprae hsp65 in autoimmune diseases is under investigation throughout the experimental autoimmune uveitis (EAU) induced by immunization of the highly susceptible B10.RIII recombinant isogenic mouse with the Interphotoreceptor Retinoid Binding Protein (IRBP), and both the humoral and cellular immune responses will be determined
  • Editor: Caxambu
  • Data de criação/publicação: 2004
  • Formato: res. C10.
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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