The membrane-anchor of Paramecium temperature-specific surface antigens is a glycosylinositol phospholipid |
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Authors: | Y Capdeville M L Cardoso de Almeida C Deregnaucourt |
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Institution: | Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique, Gif/Yvette, France. |
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Abstract: | The temperature-specific G surface antigen of Paramecium primaurelia strain 156 was biosynthetically labeled by 3H]myristic acid in its membrane-bound form, but not in its soluble form. It could be cleaved by a phosphatidylinositol-specific phospholipase C from Trypanosoma brucei or from Bacillus cereus which released its soluble form with the unmasking of a particular glycosidic immunodeterminant called the crossreacting determinant. The Paramecium enzyme, capable of converting its membrane-bound form into the soluble one, was inhibited by a sulphydril reagent in the same way as the trypanosomal lipase. From this evidence we propose that the Paramecium temperature-specific surface antigens are anchored in the plasma membrane via a glycophospholipid, and that an endogenous phospholipase C may be involved in the antigenic variation process. |
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