Role of alpha-dystroglycan as a Schwann cell receptor for Mycobacterium leprae

Science. 1998 Dec 11;282(5396):2076-9. doi: 10.1126/science.282.5396.2076.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Bacterial Adhesion*
  • Binding Sites
  • Calcium / physiology
  • Cell Line, Transformed
  • Cells, Cultured
  • Cytoskeletal Proteins / metabolism*
  • Cytoskeletal Proteins / pharmacology
  • Dystroglycans
  • Edetic Acid / pharmacology
  • Glycosylation
  • Humans
  • Laminin / chemistry
  • Laminin / metabolism*
  • Membrane Glycoproteins / metabolism*
  • Membrane Glycoproteins / pharmacology
  • Mycobacterium leprae / metabolism*
  • Peripheral Nerves / chemistry
  • Rats
  • Receptors, Laminin / metabolism
  • Recombinant Fusion Proteins / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Schwann Cells / metabolism
  • Schwann Cells / microbiology*

Substances

  • Cytoskeletal Proteins
  • DAG1 protein, human
  • Laminin
  • Membrane Glycoproteins
  • Receptors, Laminin
  • Recombinant Fusion Proteins
  • Recombinant Proteins
  • Dystroglycans
  • Edetic Acid
  • Calcium