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 Parasitoljournal_title
Experimental parasitologyauthors
Abuin G,Couto AS,de Lederkremer RM,Casal OL,Galli C,Colli W,Alves MJdoi
10.1006/expr.1996.0036subject
Has Abstractpub_date
1996-04-01 00:00:00pages
290-7issue
3eissn
0014-4894issn
1090-2449pii
S0014-4894(96)90036-3journal_volume
82pub_type
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