Molecular variation in Leishmania.

The surface coat of the protozoan parasite Leishmania affords remarkable protection in the harsh environments encountered within the insect vectors and vertebrate hosts. It also provides specificity for the interaction of these parasites with the cells in the sandfly gut and with the human macrophage. Surprisingly few molecules have been identified on the Leishmania surface. The major surface molecules of both promastigotes and amastigotes are the glycoconjugates lipophosphoglycan and a glycoprotein of approximately 63 kDa. These major surface molecules vary structurally between Leishmania species and throughout the life-cycle of the parasite. In addition to these major glycoconjugates, Leishmania produce a number of less abundant surface molecules, including a family of glycosyl-inositol phospholipids, the Promastigote Surface Antigen-2 complex of glycoproteins and a glycoprotein of M(r) 46,000. These molecules share the common feature of attachment to the plasma membrane via glycosylphosphatidylinositol lipid anchors. Leishmania also release molecules from their surface in a species specific manner. In this review we will examine the molecular variation of these molecules and their biological importance. We will also discuss the potential of these molecules as targets for chemotherapy and as candidate vaccines.