Trypanosoma cruzi: the Tc-85 surface glycoprotein shed by trypomastigotes bears a modified glycosylphosphatidylinositol anchor.

Abstract:

:Tc-85, an 85-kDa surface glycoprotein specific for the trypomastigote stage of Trypanosoma cruzi, has been implicated in the invasion of host cells by the parasite. Radioactive palmitic acid was incorporated into Tc-85 immunoprecipitated from the culture medium with the H1A10 monoclonal antibody, suggesting that shedding occurs with Tc-85 bearing its GPI anchor. In contrast to the glycoprotein remaining in the parasites, the glycosylphosphatidylinositol moiety in shed Tc-85 is resistant to phosphatidylinositol phospholipase C and becomes susceptible to the enzyme following alkali treatment. An alkylglycerol was identified by thin layer chromatography of an ether extract after the enzymatic reaction. Resistance to cleavage by phospholipase C is due to fatty acid esterification of the inositol residue in shed Tc-85. This is the first example of inositol modification in anchors from a glycoprotein of Trypanosoma cruzi.

journal_name

Exp Parasitol

authors

Abuin G,Couto AS,de Lederkremer RM,Casal OL,Galli C,Colli W,Alves MJ

doi

10.1006/expr.1996.0036

subject

Has Abstract

pub_date

1996-04-01 00:00:00

pages

290-7

issue

3

eissn

0014-4894

issn

1090-2449

pii

S0014-4894(96)90036-3

journal_volume

82

pub_type

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