Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 11 December 1998:
Vol. 282. no. 5396, pp. 2076 - 2079
DOI: 10.1126/science.282.5396.2076
Prev | Table of Contents | Next

Reports

Role of alpha -Dystroglycan as a Schwann Cell Receptor for Mycobacterium leprae

Anura Rambukkana, * Hiroki Yamada, George Zanazzi, Todd Mathus, James L. Salzer, Peter D. Yurchenco, Kevin P. Campbell, Vincent A. Fischetti

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 alpha 2 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.

A. Rambukkana and V. A. Fischetti, Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, NY 10021, U.S.A. H. Yamada and K. P. Campbell, Howard Hughes Medical Institute, (HHMI), Department of Physiology and Biophysics, and Department of Neurology, University of Iowa College of Medicine, Iowa City, IA 52242, U.S.A. G. Zanazzi and J. L. Salzer, Departments of Cell Biology and Neurology and the Kaplan Cancer Center, New York University Medical Center, New York, NY 10016, U.S.A. T. Mathus and P. D. Yurchenco, Department of Pathology, Robert Wood Johnson Medical School, Piscataway, NJ 08854, U.S.A.
*   To whom correspondence should be addressed. E-mail: rambuka{at}rockvax.rockefeller.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Inaugural Article: Basal lamina strengthens cell membrane integrity via the laminin G domain-binding motif of {alpha}-dystroglycan.
R. Han, M. Kanagawa, T. Yoshida-Moriguchi, E. P. Rader, R. A. Ng, D. E. Michele, D. E. Muirhead, S. Kunz, S. A. Moore, S. T. Iannaccone, et al. (2009)
PNAS 106, 12573-12579
   Abstract »    Full Text »    PDF »
Post-translational modification of {alpha}-dystroglycan is not critical for lymphocytic choriomeningitis virus receptor function in vivo.
M. Imperiali, R. Sporri, J. Hewitt, and A. Oxenius (2008)
J. Gen. Virol. 89, 2713-2722
   Abstract »    Full Text »    PDF »
Angiogenesis in Cutaneous Lesions of Leprosy: Implications for Treatment.
S. S. Bhandarkar, C. Cohen, M. Kuruvila, T. H. Rea, J. B. MacKelfresh, D. J. Lee, R. L. Modlin, and J. L. Arbiser (2007)
Arch Dermatol 143, 1527-1529
   Abstract »    Full Text »    PDF »
A Newly Identified Leptospiral Adhesin Mediates Attachment to Laminin.
A. S. Barbosa, P. A. E. Abreu, F. O. Neves, M. V. Atzingen, M. M. Watanabe, M. L. Vieira, Z. M. Morais, S. A. Vasconcellos, and A. L. T. O. Nascimento (2006)
Infect. Immun. 74, 6356-6364
   Abstract »    Full Text »    PDF »
Role of non-raft cholesterol in lymphocytic choriomeningitis virus infection via {alpha}-dystroglycan..
W. A. Shah, H. Peng, and S. Carbonetto (2006)
J. Gen. Virol. 87, 673-678
   Abstract »    Full Text »    PDF »
Dystroglycan: from biosynthesis to pathogenesis of human disease.
R. Barresi and K. P. Campbell (2006)
J. Cell Sci. 119, 199-207
   Abstract »    Full Text »    PDF »
O Mannosylation of {alpha}-Dystroglycan Is Essential for Lymphocytic Choriomeningitis Virus Receptor Function.
M. Imperiali, C. Thoma, E. Pavoni, A. Brancaccio, N. Callewaert, and A. Oxenius (2005)
J. Virol. 79, 14297-14308
   Abstract »    Full Text »    PDF »
The Structure of the N-terminal Region of Murine Skeletal Muscle {alpha}-Dystroglycan Discloses a Modular Architecture.
D. Bozic, F. Sciandra, D. Lamba, and A. Brancaccio (2004)
J. Biol. Chem. 279, 44812-44816
   Abstract »    Full Text »    PDF »
Proteolytic Enzymes and Altered Glycosylation Modulate Dystroglycan Function in Carcinoma Cells.
J. Singh, Y. Itahana, S. Knight-Krajewski, M. Kanagawa, K. P. Campbell, M. J. Bissell, and J. Muschler (2004)
Cancer Res. 64, 6152-6159
   Abstract »    Full Text »    PDF »
Loss of basement membrane, receptor and cytoskeletal lattices in a laminin-deficient muscular dystrophy.
P. D. Yurchenco, Y.-S. Cheng, K. Campbell, and S. Li (2004)
J. Cell Sci. 117, 735-742
   Abstract »    Full Text »    PDF »
Case 1-2004 - A 49-Year-Old Woman with Asymmetric Painful Neuropathy.
D. A. Chad and E. T. Hedley-Whyte (2004)
N. Engl. J. Med. 350, 166-176
   Full Text »    PDF »
Targeting Schwann cells by nonlytic arenaviral infection selectively inhibits myelination.
A. Rambukkana, S. Kunz, J. Min, K. P. Campbell, and M. B. A. Oldstone (2003)
PNAS 100, 16071-16076
   Abstract »    Full Text »    PDF »
Dystroglycan glycosylation and its role in matrix binding in skeletal muscle.
P. T. Martin (2003)
Glycobiology 13, 55R-66R
   Abstract »    Full Text »    PDF »
Identification of a Treponema pallidum Laminin-Binding Protein.
C. E. Cameron (2003)
Infect. Immun. 71, 2525-2533
   Abstract »    Full Text »    PDF »
Contributions of the LG Modules and Furin Processing to Laminin-2 Functions.
S. P. Smirnov, E. L. McDearmon, S. Li, J. M. Ervasti, K. Tryggvason, and P. D. Yurchenco (2002)
J. Biol. Chem. 277, 18928-18937
   Abstract »    Full Text »    PDF »
Trypanosoma cruzi trans-sialidase: A potent and specific survival factor for human Schwann cells by means of phosphatidylinositol 3-kinase/Akt signaling.
M. V. Chuenkova, F. B. Furnari, W. K. Cavenee, and M. A. Pereira (2001)
PNAS
   Abstract »    Full Text »    PDF »
Processing of {beta}-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex.
H. Yamada, F. Saito, H. Fukuta-Ohi, D. Zhong, A. Hase, K. Arai, A. Okuyama, R. Maekawa, T. Shimizu, and K. Matsumura (2001)
Hum. Mol. Genet. 10, 1563-1569
   Abstract »    Full Text »    PDF »
Mycobacterium leprae-Specific, HLA Class II-Restricted Killing of Human Schwann Cells by CD4+ Th1 Cells: A Novel Immunopathogenic Mechanism of Nerve Damage in Leprosy.
E. Spierings, T. de Boer, B. Wieles, L. B. Adams, E. Marani, and T. H. M. Ottenhoff (2001)
J. Immunol. 166, 5883-5888
   Abstract »    Full Text »    PDF »
A new {{beta}}-1,2-N-acetylglucosaminyltransferase that may play a role in the biosynthesis of mammalian O-mannosyl glycans.
S. Takahashi, T. Sasaki, H. Manya, Y. Chiba, A. Yoshida, M. Mizuno, H.-K. Ishida, F. Ito, T. Inazu, N. Kotani, et al. (2001)
Glycobiology 11, 37-45
   Abstract »    Full Text »    PDF »
Presentation of chemokine SDF-1alpha by fibronectin mediates directed migration of T cells.
A. J. Pelletier, L. J. W. van der Laan, P. Hildbrand, M. A. Siani, D. A. Thompson, P. E. Dawson, B. E. Torbett, and D. R. Salomon (2000)
Blood 96, 2682-2690
   Abstract »    Full Text »    PDF »
The Role of Dystroglycan and Its Ligands in Physiology and Disease.
T. Meier and M. A. Ruegg (2000)
Physiology 15, 255-259
   Abstract »    Full Text »    PDF »
Genomic Organization of the Dog Dystroglycan Gene DAG1 Locus on Chromosome 20q15.1-q15.2.
T. Leeb, S. Neumann, A. Deppe, M. Breen, and B. Brenig (2000)
Genome Res. 10, 295-301
   Abstract »    Full Text »
The Small Leucine-Rich Repeat Proteoglycan Biglycan Binds to {alpha}-Dystroglycan and Is Upregulated in Dystrophic Muscle.
M. A. Bowe, D. B. Mendis, and J. R. Fallon (2000)
J. Cell Biol. 148, 801-810
   Abstract »    Full Text »    PDF »
Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin.
M James, A Nuttall, J. Ilsley, K Ottersbach, J. Tinsley, M Sudol, and S. Winder (2000)
J. Cell Sci. 113, 1717-1726
   Abstract »    PDF »
A 21-kDa surface protein of Mycobacterium leprae binds peripheral nerve laminin-2 and mediates Schwann cell invasion.
Y. Shimoji, V. Ng, K. Matsumura, V. A. Fischetti, and A. Rambukkana (1999)
PNAS 96, 9857-9862
   Abstract »    Full Text »    PDF »
Structural and Functional Analysis of the Recombinant G Domain of the Laminin alpha 4 Chain and Its Proteolytic Processing in Tissues.
J. F. Talts, T. Sasaki, N. Miosge, W. Gohring, K. Mann, R. Mayne, and R. Timpl (2000)
J. Biol. Chem. 275, 35192-35199
   Abstract »    Full Text »    PDF »
Trypanosoma cruzi trans-sialidase: A potent and specific survival factor for human Schwann cells by means of phosphatidylinositol 3-kinase/Akt signaling.
M. V. Chuenkova, F. B. Furnari, W. K. Cavenee, and M. A. Pereira (2001)
PNAS 98, 9936-9941
   Abstract »    Full Text »    PDF »
Molecular analysis of the interaction of LCMV with its cellular receptor {alpha}-dystroglycan.
S. Kunz, N. Sevilla, D. B. McGavern, K. P. Campbell, and M. B.A. Oldstone (2001)
J. Cell Biol. 155, 301-310
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)