Leishmania and Trypanosoma surface glycoproteins have a common glycophospholipid membrane anchor.

Abstract

The variant surface glycoprotein (VSG) of the African trypanosomes is the major membrane protein of the plasma membrane of the bloodstream stage of the parasite. It is anchored in the plasma membrane by a glycolipid covalently bound to the C-terminal amino acid of the protein. The VSG is released through the action of a phosphatidylinositol-specific phospholipase C that removes dimyristoylglycerol and exposes the carbohydrate antigenic determinant common to all VSGs. Promastigotes of Leishmania have a predominant surface glycoprotein, termed p63, that is anchored in the plasma membrane in a similar way. A water-soluble form of p63 can be generated through the action of phosphatidylinositol-specific phospholipase C from trypanosomes or from Bacillus cereus. Either treatment exposes on the Leishmania p63 an antigenic determinant recognized by antibody prepared against the trypanosomal crossreacting determinant. These findings indicate that p63 and VSG have a common membrane anchor and are structurally related.