THE GP120 GLYCOPROTEIN OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 BINDS TO SENSORY GANGLION NEURONS

Using immunofluorescence microscopy we found that gp120 binds to the s urface of rat dorsal root ganglia neurons and human neuroblastoma cell s but not to rat fibroblasts or glial cells. The binding of gp120 to n eurons was eliminated by pretreatment with trypsin, which removes cell -surface proteins, but not with chloroform: methanol, which removes gl ycolipids. As control, neuronal staining by antisulfatide antibodies w as eliminated by pretreatment with chloroform:methanol but not with tr ypsin. The gp120 binding to neurons was also inhibited by the mouse mo noclonal antibody 01, which binds to galactocerebroside and cross-reac tive glycoproteins. These studies suggest that the receptor for gp120 on the surface of the dorsal root ganglia neurons is a glycoprotein. T his interaction may mediate the effects of human immunodeficiency viru s type 1 in sensory neuropathy.