Characteristics of the minor group receptor of human rhinoviruses.

The receptor for the minor group of human rhinoviruses was solubilized from HeLa cell membranes with various detergents. Virus binding activity was determined in a filter binding assay using 35S-labeled human rhinovirus 2 (HRV2) as a probe. The receptor protein was enriched on Lens culinaris lectin columns and the active fractions were further purified by gel permeation and anion exchange chromatography. The receptor has an apparent molecular weight of 450 kDa in the presence of detergent. The binding activity is sensitive to trypsin, sulfhydryl modifying agents, but insensitive to neuraminidase. Divalent cations are essential for virus binding.