Immunochemical characterization of a glyco-inositol-phospholipid membrane antigen of Leishmania major.

A low m.w. polymorphic glyco-inositol-phospholipid (GIPL) of Leishmania major was studied by using three different mAb. This molecule is shown to be distinct from the previously described lipophosphoglycan of L. major in its m.w., antigenic properties, expression during parasite growth, and kinetics of synthesis and catabolism. GIPL is shown to be released from the parasite surface in a water-soluble form, probably by an endogenous phospholipase. GIPL is also detectable on the surface of infected macrophages, although not all epitopes are detectable in this state. GIPL can be metabolically labeled with [3H]galactose, [3H]inositol, [32P]phosphate, and [3H]palmitic acid. GIPL can also be labeled on the surface of living promastigotes with galactose oxidase and [3H]sodium borohydride. The kinetics of synthesis and catabolism are much faster than those of lipophosphoglycan. GIPL is sensitive to degradation upon parasite lysis and becomes undetectable by mAb after 20 h at 37 degrees C. The expression of GIPL on the surface of promastigotes is more abundant during the logarithmic phase of growth, and declines in stationary phase.