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A peripheral membrane protein that is interactive with lymphocytic choriomeningitis virus (LCMV) was purified from cells permissive to infection. Tryptic peptides from this protein were determined to be alpha-dystroglycan (alpha-DG). Several strains of LCMV and other arenaviruses, including Lassa fever virus (LFV), Oliveros, and Mobala, bound to purified alpha-DG protein. Soluble alpha-DG blocked both LCMV and LFV infection. Cells bearing a null mutation of the gene encoding DG were resistant to LCMV infection, and reconstitution of DG expression in null mutant cells restored susceptibility to LCMV infection. Thus, alpha-DG is a cellular receptor for both LCMV and LFV.


Journal article



Publication Date





2079 - 2081


Amino Acid Sequence, Animals, Arenavirus, Cell Line, Cytoskeletal Proteins, Dystroglycans, Lassa virus, Lymphocytic choriomeningitis virus, Membrane Glycoproteins, Mice, Molecular Sequence Data, Mutation, Receptors, Virus, Recombinant Fusion Proteins, Virus Replication