TY - JOUR KW - Animals KW - Bacterial Adhesion KW - Humans KW - Immunohistochemistry KW - Laminin KW - Mycobacterium KW - Mycobacterium chelonae KW - Mycobacterium leprae KW - Mycobacterium smegmatis KW - Mycobacterium tuberculosis KW - Schwann Cells KW - Tumor Cells, Cultured AU - Marques M A AU - Ant nio V L AU - Sarno E N AU - Brennan P J AU - Pessolani M C AB -

The ability of Mycobacterium leprae to specifically bind alpha2-laminins of Schwann cells has been described recently as being an important property of the leprosy bacillus, which could explain the neural tropism of M. leprae. Therefore, the extent of the expression of alpha2-laminin-binding properties among mycobacteria was investigated. In an ELISA-based assay, all three species of Mycobacterium tested (M. tuberculosis, M. chelonae and M. smegmatis) expressed laminin-binding capacity, suggesting that the ability to bind alpha2-laminins is conserved within the genus Mycobacterium. This report also demonstrated that not only M. leprae but all the mycobacterial species tested readily interacted with the ST88-14 cells, a human schwannoma cell line, and that the addition of soluble alpha2-laminins significantly increased their adherence to these cells. These results failed to demonstrate the presence in M. leprae of a unique system based on alpha2-laminins for adherence to Schwann cells.

BT - Journal of medical microbiology C1 - http://www.ncbi.nlm.nih.gov/pubmed/11192500?dopt=Abstract DA - 2001 Jan DO - 10.1099/0022-1317-50-1-23 IS - 1 J2 - J. Med. Microbiol. LA - eng N2 -

The ability of Mycobacterium leprae to specifically bind alpha2-laminins of Schwann cells has been described recently as being an important property of the leprosy bacillus, which could explain the neural tropism of M. leprae. Therefore, the extent of the expression of alpha2-laminin-binding properties among mycobacteria was investigated. In an ELISA-based assay, all three species of Mycobacterium tested (M. tuberculosis, M. chelonae and M. smegmatis) expressed laminin-binding capacity, suggesting that the ability to bind alpha2-laminins is conserved within the genus Mycobacterium. This report also demonstrated that not only M. leprae but all the mycobacterial species tested readily interacted with the ST88-14 cells, a human schwannoma cell line, and that the addition of soluble alpha2-laminins significantly increased their adherence to these cells. These results failed to demonstrate the presence in M. leprae of a unique system based on alpha2-laminins for adherence to Schwann cells.

PY - 2001 SP - 23 EP - 8 T2 - Journal of medical microbiology TI - Binding of alpha2-laminins by pathogenic and non-pathogenic mycobacteria and adherence to Schwann cells. VL - 50 SN - 0022-2615 ER -