[HTML][HTML] Bacterial and host-derived cationic proteins bind α2-laminins and enhance Mycobacterium leprae attachment to human Schwann cells
MA de Melo Marques, S Mahapatra, D Nandan… - Microbes and …, 2000 - Elsevier
It has recently been demonstrated that laminin α2 chains present on the surface of Schwann
cells are involved in the process of attachment of Mycobacterium leprae to these cells. In this
study, a protein in the M. leprae cell wall that was found to be capable of binding α2-
containing laminins (merosin) was isolated and characterized. The M. leprae laminin-
binding protein was identified as a 21-kDa histone-like protein (Hlp), a highly conserved
cationic protein present in other species of mycobacteria. The gene that encodes this protein …
cells are involved in the process of attachment of Mycobacterium leprae to these cells. In this
study, a protein in the M. leprae cell wall that was found to be capable of binding α2-
containing laminins (merosin) was isolated and characterized. The M. leprae laminin-
binding protein was identified as a 21-kDa histone-like protein (Hlp), a highly conserved
cationic protein present in other species of mycobacteria. The gene that encodes this protein …