Binding of alpha2-laminins by pathogenic and non-pathogenic mycobacteria and adherence to Schwann cells.
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.
Marques
M A
MA
Laboratório de Hanseníase, Fundaçao Oswaldo Cruz, Rio de Janeiro, RJ, Brazil.
Ant nio
V L
VL
Sarno
E N
EN
Brennan
P J
PJ
Pessolani
M C
MC
D000818:Animals; D001422:Bacterial Adhesion; D006801:Humans; D007150:Immunohistochemistry; D007797:Laminin / Q000378:metabolism*; D009161:Mycobacterium / Q000378:metabolism* / Q000502:physiology; D016926:Mycobacterium chelonae / Q000378:metabolism / Q000502:physiology; D009166:Mycobacterium leprae / Q000378:metabolism / Q000502:physiology; D020102:Mycobacterium smegmatis / Q000378:metabolism / Q000502:physiology; D009169:Mycobacterium tuberculosis / Q000378:metabolism / Q000502:physiology; D012583:Schwann Cells / Q000382:microbiology*; D014407:Tumor Cells, Cultured
D007797:Laminin; C102645:laminin alpha 2