The gp 120 glycoprotein of human immunodeficiency virus type 1 binds to sensory ganglion neurons

Using immunofluorescence microscopy we found that gp 120 binds to the surface of rat dorsal root ganglia neurons and human neuroblastoma cells but not to rat fibroblasts or glial cells. The binding of gp 120 to neurons was eliminated by pretreatment with trypsin, which removes cell-surface proteins, but not with chloroform: methanol, which removes glycolipids. As control, neuronal staining by antisulfatide antibodies was eliminated by pretreatment with chloroform: methanol but not with trypsin. The gp 120 binding to neurons was also inhibited by the mouse monoclonal antibody 01, which binds to galactocerebroside and cross-reactive glycoproteins. These studies suggest that the receptor for gp 120 on the surface of the dorsal root ganglia neurons is a glycoprotein. This interaction may mediate the effects of human immunodeficiency virus type 1 in sensory neuropathy.