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. 1993 Nov;67(11):6889–6892. doi: 10.1128/jvi.67.11.6889-6892.1993

Generation of a water-soluble oligomeric ectodomain of the Rous sarcoma virus envelope glycoprotein.

J M Gilbert 1, L D Hernandez 1, T Chernov-Rogan 1, J M White 1
PMCID: PMC238138  PMID: 7692089

Abstract

Sequences encoding the transmembrane domain of the Rous sarcoma virus envelope (Env) glycoprotein were deleted and replaced with sequences that signal addition of a glycosyl phosphatidylinositol (GPI) membrane anchor. Stable NIH 3T3 cell lines expressing either the wild-type transmembrane-anchored Env or the Env chimera with a GPI tail were established. The GPI-anchored envelope glycoprotein is expressed, oligomerized, and transported to the cell surface in a manner identical to that of its wild-type transmembrane-anchored counterpart. The GPI-linked protein is quantitatively removed from the cell surface by treatment with phosphatidylinositol phospholipase C. The phosphatidylinositol phospholipase C-released, water-soluble Env glycoprotein ectodomain retains the wild-type oligomeric structure and provides a useful tool for studying the subgroup-specific binding and fusion activities of a prototypic retroviral Env glycoprotein.

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