| Title | Role of alpha-dystroglycan as a Schwann cell receptor for Mycobacterium leprae. |
| Publication Type | Journal Article |
| Year of Publication | 1998 |
| Authors | Rambukkana A, Yamada H, Zanazzi G, Mathus T, Salzer JL, Yurchenco PD, Campbell KP, Fischetti VA |
| Journal | Science |
| Volume | 282 |
| Issue | 5396 |
| Pagination | 2076-9 |
| Date Published | 1998 Dec 11 |
| ISSN | 0036-8075 |
| Keywords | Animals, Bacterial Adhesion, Binding Sites, Calcium, Cell Line, Transformed, Cells, Cultured, Cytoskeletal Proteins, Dystroglycans, Edetic Acid, Glycosylation, Humans, Laminin, Membrane Glycoproteins, Mycobacterium leprae, Peripheral Nerves, Rats, Receptors, Laminin, Recombinant Fusion Proteins, Recombinant Proteins, Schwann Cells |
| Abstract | alpha-Dystroglycan (alpha-DG) is a component of the dystroglycan complex, which is involved in early development and morphogenesis and in the pathogenesis of muscular dystrophies. Here, alpha-DG was shown to serve as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy. Mycobacterium leprae specifically bound to alpha-DG only in the presence of the G domain of the alpha2 chain of laminin-2. Native alpha-DG competitively inhibited the laminin-2-mediated M. leprae binding to primary Schwann cells. Thus, M. leprae may use linkage between the extracellular matrix and cytoskeleton through laminin-2 and alpha-DG for its interaction with Schwann cells. |
| Alternate Journal | Science |
| PubMed ID | 9851927 |
Publication institute:
Other
Printer-friendly version