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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.

Type

Journal article

Journal

Science

Publication Date

11/12/1998

Volume

282

Pages

2079 - 2081

Keywords

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