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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Bacterial Adhesion*
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Binding Sites
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Calcium / physiology
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Cell Line, Transformed
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Cells, Cultured
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Cytoskeletal Proteins / metabolism*
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Cytoskeletal Proteins / pharmacology
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Dystroglycans
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Edetic Acid / pharmacology
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Glycosylation
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Humans
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Laminin / chemistry
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Laminin / metabolism*
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Membrane Glycoproteins / metabolism*
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Membrane Glycoproteins / pharmacology
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Mycobacterium leprae / metabolism*
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Peripheral Nerves / chemistry
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Rats
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Receptors, Laminin / metabolism
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Schwann Cells / metabolism
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Schwann Cells / microbiology*
Substances
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Cytoskeletal Proteins
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DAG1 protein, human
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Laminin
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Membrane Glycoproteins
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Receptors, Laminin
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Recombinant Fusion Proteins
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Recombinant Proteins
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Dystroglycans
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Edetic Acid
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Calcium