Further biochemical characterization of Mycobacterium leprae laminin-binding proteins

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Abstract

It has been demonstrated that the α2 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 α2-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 α2-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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Marques, M. A. M., Mahapatra, S., Sarno, E. N., Santos, S., Spencer, J. S., Brennan, P. J., & Pessolani, M. C. V. (2001). Further biochemical characterization of Mycobacterium leprae laminin-binding proteins. Brazilian Journal of Medical and Biological Research, 34(4), 463–470. https://doi.org/10.1590/S0100-879X2001000400004

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