Science · 1998 · 710 citations · 15 references
Life SciencesImmunologyInfectious DiseasesImmunology Of Infectious DiseasesMolecular VirologyVirologyAnimal VirusesAntiviral ImmunityViral InfectionsViral PathogenesisViral PathologyViral TropismAnimal Viral PathogenesisLymphocytic ChoriomeningitisPeripheral Membrane ProteinsViral Envelope GlycoproteinsViral Envelope ProteinsViral Receptor Binding DomainsViral Receptor UsageViral Surface Proteins
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.
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