Abstract
The surface of amastigotes of Trypanosoma cruzi is covered by Ssp-4, a major stage-specific glycoprotein. Ssp-4 is anchored to the cell membrane by GPI. It can be metabolically labeled with [3H]myristic acid, and is converted into a hydrophilic form by treatment with the glycan-specific phospholipase C of T. brucei, or after lysis of the parasites in non-ionic detergents. The hydrophilic form of Ssp-4 is recognized by antibodies to the cross-reactive determinant of the variant surface glycoprotein of African trypanosomes. Ssp-4 is progressively shed during the intra- or extracellular development of amastigotes preceding their transformation into epi- and trypomastigotes. We show here that T. cruzi contains a phospholipase C and that most shed Ssp-4 is hydrophilic, does not contain myristic acid, and reacts with anti-CRD. These observations provide strong evidence that phospholipase C mediates the release of this glycosyl-phosphatidylinositol-anchored protein under physiological conditions, as the parasite undergoes differentiation.
MeSH Terms
Animals
Antigens, Surface/isolation & purification
Cell Differentiation
Cell Membrane/metabolism
Glycosylation
Molecular Weight
Phosphatidylinositols/physiology
Trypanosoma cruzi/enzymology,growth & development,metabolism
Type C Phospholipases/physiology
Variant Surface Glycoproteins, Trypanosoma/isolation & purification,metabolism
Chemicals
Antigens, Surface
Phosphatidylinositols
Variant Surface Glycoproteins, Trypanosoma
Type C Phospholipases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Andrews N W
Department of Pathology, New York University Medical Center 10016.
Robbins E S
Ley V
Hong K S
Nussenzweig V
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