The trans-sialidase of Trypanosoma cruzi is anchored by two different lipids

Abstract

The trans-sialidase from the trypomastigote stage of Trypanosoma cruzi was metabolically labeled with [3H]-palmitic acid and purified by immunoprecipitation with a monoclonal antibody. The action of PI-PLC on the immunoprecipitate released a lipid that was analyzed by TLC. Lyso-1-O-hexadecylglycerol and N-palmitoyl-sphinganine were obtained in a 1:3 ratio. A comparison with the GPI anchors present in the different stages of T. cruzi was made.