Cleavage of the glycosylphosphatidylinositol anchor affects the reactivity of Thy-1 with antibodies

Tova Kukulansky, Shirley Abramovitch, Nurit Hollander*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Thy-1 protein, a member of the Ig superfamily, is bound to the cell membrane by a glycosylphosphatidylinositol (GPI) anchor. We demonstrate that following anchor cleavage by phospholipase C, the reactivity of the solubilized Thy-1 with several mAbs is lost, and its reactivity with polyclonal anti-Thy-1 Abs is markedly decreased. Hence, solubilized Thy-1 cannot be detected by a range of mAbs. In contrast, enzymatic cleavage of biotinylated Thy-1 yields an intact solubilized protein that can be detected by streptavidin. These results exclude a possible proteolytic degradation of solubilized Thy-1 and suggest that the marked decrease in Thy-1 immunoreactivity following delipidation is due to conformational changes in the Thy-1 protein. We further demonstrate that addition of phospholipase C to preformed Ab-Ag complexes causes dissociation and removal of Thy-1 from the complex, indicating that delipidation of Thy-1 induces a conformational change in Thy-1 that is sufficient to dissociate bound Ab. The possibility should therefore be considered that the GPI anchor affects the conformation of a protein to which it is linked.

Original languageEnglish
Pages (from-to)5993-5997
Number of pages5
JournalJournal of Immunology
Issue number10
StatePublished - 15 May 1999


Dive into the research topics of 'Cleavage of the glycosylphosphatidylinositol anchor affects the reactivity of Thy-1 with antibodies'. Together they form a unique fingerprint.

Cite this