{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T01:52:00Z","timestamp":1791251520502,"version":"4.1.0"},"reference-count":41,"publisher":"Rockefeller University Press","issue":"2","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2001,10,15]]},"abstract":"<jats:p>\u03b1-Dystroglycan (DG) has been identified as the cellular receptor for lymphocytic choriomeningitis virus (LCMV) and Lassa fever virus (LFV). This subunit of DG is a highly versatile cell surface molecule that provides a molecular link between the extracellular matrix (ECM) and a \u03b2-DG transmembrane component, which interacts with the actin-based cytoskeleton. In addition, DG exhibits a complex pattern of interaction with a wide variety of ECM and cellular proteins. In the present study, we characterized the binding of LCMV to \u03b1-DG and addressed the role of \u03b1-DG\u2013associated host-derived proteins in virus infection. We found that the COOH-terminal region of \u03b1-DG's first globular domain and the NH2-terminal region of the mucin-related structures of \u03b1-DG together form the binding site for LCMV. The virus\u2013\u03b1-DG binding unlike ECM \u03b1-DG interactions was not dependent on divalent cations. Despite such differences in binding, LCMV and laminin-1 use, in part, an overlapping binding site on \u03b1-DG, and the ability of an LCMV isolate to compete with laminin-1 for receptor binding is determined by its binding affinity to \u03b1-DG. This competition of the virus with ECM molecules for receptor binding likely explains the recently found correlation between the affinity of LCMV binding to \u03b1-DG, tissue tropism, and pathological potential. LCMV strains and variants with high binding affinity to \u03b1-DG but not low affinity binders are able to infect CD11c+ dendritic cells, which express \u03b1-DG at their surface. Infection followed by dysfunction of these antigen-presenting cells contributes to immunosuppression and persistent viral infection in vivo.<\/jats:p>","DOI":"10.1083\/jcb.200104103","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T12:46:23Z","timestamp":1027687583000},"page":"301-310","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":140,"title":["Molecular analysis of the interaction of LCMV with its cellular receptor\n                    <b>\u03b1<\/b>\n                    -dystroglycan"],"prefix":"10.1083","volume":"155","author":[{"given":"Stefan","family":"Kunz","sequence":"first","affiliation":[{"name":"1The Scripps Research Institute, Division of Virology, Department of Neuropharmacology, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noemi\u0301","family":"Sevilla","sequence":"additional","affiliation":[{"name":"1The Scripps Research Institute, Division of Virology, Department of Neuropharmacology, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dorian B.","family":"McGavern","sequence":"additional","affiliation":[{"name":"1The Scripps Research Institute, Division of Virology, Department of Neuropharmacology, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin P.","family":"Campbell","sequence":"additional","affiliation":[{"name":"2Howard Hughes Medical Institute, University of Iowa College of Medicine, Department of Physiology and Biophysics, Neurology, Iowa City, IA 52242"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael B.A.","family":"Oldstone","sequence":"additional","affiliation":[{"name":"1The Scripps Research Institute, Division of Virology, Department of Neuropharmacology, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[2001,10,15]]},"reference":[{"key":"2023072211572073300_BIB1","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1084\/jem.160.2.521","volume":"160","year":"1984","journal-title":"J. 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