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The gp 120 glycoprotein of human immunodeficiency virus type 1 binds to sensory ganglion neurons
Author(s) -
Apostolski Slobodan,
McAlarney Terence,
Quattrini Angelo,
Levison Steven W.,
Rosoklija Gorazd,
Lugaressi Alessandra,
Corbo Massimo,
Sadiq Saud A.,
Lederman Seth,
Hays Arthur P.,
Latov Norman
Publication year - 1993
Publication title -
annals of neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.764
H-Index - 296
eISSN - 1531-8249
pISSN - 0364-5134
DOI - 10.1002/ana.410340616
Subject(s) - dorsal root ganglion , glycoprotein , galactocerebroside , microbiology and biotechnology , immunofluorescence , lectin , monoclonal antibody , biology , trypsin , concanavalin a , cell culture , antibody , chemistry , biochemistry , central nervous system , sensory system , immunology , endocrinology , neuroscience , in vitro , myelin , genetics , oligodendrocyte , enzyme
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.