Registro completo |
Provedor de dados: |
BJMBR
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País: |
Brazil
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Título: |
Further biochemical characterization of Mycobacterium leprae laminin-binding proteins
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Autores: |
Marques,M.A.M.
Mahapatra,S.
Sarno,E.N.
Santos,S.
Spencer,J.S.
Brennan,P.J.
Pessolani,M.C.V.
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Data: |
2001-04-01
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Ano: |
2001
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Palavras-chave: |
Mycobacterium leprae
Laminin
Adhesion
Schwann cell
Ribosomal protein
Histone
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Resumo: |
It has been demonstrated that the alpha2 chain of laminin-2 present on the surface of Schwann cells is involved in the process of attachment of Mycobacterium leprae to these cells. Searching for M. leprae laminin-binding molecules, in a previous study we isolated and characterized the cationic proteins histone-like protein (Hlp) and ribosomal proteins S4 and S5 as potential adhesins involved in M. leprae-Schwann cell interaction. Hlp was shown to bind alpha2-laminins and to greatly enhance the attachment of mycobacteria to ST88-14 Schwann cells. In the present study, we investigated the laminin-binding capacity of the ribosomal proteins S4 and S5. The genes coding for these proteins were PCR amplified and their recombinant products were shown to bind alpha2-laminins in overlay assays. However, when tested in ELISA-based assays and in adhesion assays with ST88-14 cells, in contrast to Hlp, S4 and S5 failed to bind laminin and act as adhesins. The laminin-binding property and adhesin capacity of two basic host-derived proteins were also tested, and only histones, but not cytochrome c, were able to increase bacterial attachment to ST88-14 cells. Our data suggest that the alanine/lysine-rich sequences shared by Hlp and eukaryotic H1 histones might be involved in the binding of these cationic proteins to laminin.
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Tipo: |
Info:eu-repo/semantics/article
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Idioma: |
Inglês
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Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001000400004
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Editor: |
Associação Brasileira de Divulgação Científica
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Relação: |
10.1590/S0100-879X2001000400004
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Formato: |
text/html
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Fonte: |
Brazilian Journal of Medical and Biological Research v.34 n.4 2001
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Direitos: |
info:eu-repo/semantics/openAccess
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