A 21-kDa surface protein of Mycobacterium leprae binds peripheral nerve laminin-2 and mediates Schwann cell invasion

• DOI: 10.1073/pnas.96.17.9857
• Publication Date: 2002-07-26T14:38:21Z
• Authors: Yoshihiro Shimoji; Vincent Ng; Kiichiro Matsumura; Vincent A. Fischetti; Anura Rambukkana
• Keywords: Mycobacterium leprae; Schwann cell; Immunoelectron microscopy

Nerve damage is the hallmark of Mycobacterium leprae infection, which results from M. invasion Schwann cell peripheral nervous system. We have recently shown that laminin-2 isoform, specially G domain laminin α2 chain, on cell–axon unit serves as an initial neural target for . However, surface molecules mediate bacterial nerves are entirely unknown. By using human laminins a probe, major 28-kDa protein in wall fraction binds was identified. After N-terminal amino acid sequence analysis, PCR-based strategy used to clone gene encodes this protein. Deduced laminin-binding predicts 21-kDa molecule (ML-LBP21), smaller than observed molecular size SDS/PAGE. Immunofluorescence and immunoelectron microscopy intact with mAbs against recombinant (r) ML-LBP21 revealed exposed. rML-LBP21 avidly bound laminins, rG laminin-α2 native nerve laminin-2. The role adhesion investigated by fluorescent polystyrene beads coated rML-LBP21. Although alone specifically adhered were ingested primary cells, these functions significantly enhanced when preincubated exogenous laminins. Taken together, present data suggest may function critical adhesin facilitates entry into cells.