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Journal of Neuroscience, Vol 13, 941-951, Copyright © 1993 by Society for Neuroscience
HSV-1 vector-mediated gene transfer of the human nerve growth factor receptor p75hNGFR defines high-affinity NGF binding
DS Battleman, AI Geller and MV Chao
Department of Cell Biology and Anatomy, Cornell University Medical College, New York, New York 10021.
A series of recombinant herpes simplex virus (HSV-1) vectors have been
constructed that encode either the full-length cDNA of the human p75 NGF
receptor (p75hNGFR) or truncated forms of the receptor. Infection of
cultured fibroblast cells with viral stocks results in abundant expression
of all three cDNAs, as detected by affinity cross-linking, immunoblot
analysis, and equilibrium binding. Furthermore, viral infection of primary
neuronal cultures gives easily detectable p75 expression by
immunofluorescence and affinity cross-linking. When p75 was introduced by
viral infection into fibroblast cells expressing the trk proto-oncogene, a
new binding site was created, consistent with high-affinity NGF binding.
This site is not created by the coexpression of truncated forms of p75 that
lack either the extracellular ligand binding domain or the cytoplasmic
domain of the receptor, suggesting that both of these regions of the
receptor are required for the formation of the high-affinity NGF binding
site. Hence, these HSV-1 vectors give rise to appropriate NGF receptor
binding after viral infection. The application of these HSV-1 constructs to
primary neuronal culture and in vivo models of p75NGFR function is
discussed.
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