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,...

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Veröffentlicht in:Annals of neurology 1993-12, Vol.34 (6), p.855-863
Hauptverfasser: 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
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container_end_page 863
container_issue 6
container_start_page 855
container_title Annals of neurology
container_volume 34
creator 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
description 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.
doi_str_mv 10.1002/ana.410340616
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title The gp 120 glycoprotein of human immunodeficiency virus type 1 binds to sensory ganglion neurons
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