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Volume 270, Number 13, Issue of March 31, 1995 pp. 7241-7250
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Structural Characterization of the Major Glycosylphosphatidylinositol Membrane-anchored Glycoprotein from Epimastigote Forms of Trypanosoma cruzi Y-strain

(Received for publication, November 23, 1994; and in revised form, January 9, 1995)

José O. Previato ,  Christopher Jones ,  Marcia T. Xavier ,  Robin Wait ,  Luiz R. Travassos ,  Armando J. Parodi ,  Lucia Mendonça-Previato

We have investigated the structure of the glycosylphosphatidylinositol (GPI) anchor and the O-linked glycan chains of the 40/45-kDa glycoprotein from the cell surface of the protozoan parasite Trypanosoma cruzi. This glycoconjugate is the major acceptor for sialic acid transferred by trans-sialidase of T. cruzi Y-strain, epimastigote form. The GPI anchor was liberated by treatment with hot alkali, and the phosphoinositol-oligosaccharide moiety was characterized and shown to have the following structure.

Usually the glucosamine was 6-O-substituted with 2-aminoethylphosphonate, and 2-aminoethylphosphonate was also present on the third mannose residue distal to glucosamine, partially replacing the ethanolamine phosphate. The beta-eliminated reduced oligosaccharide chains showed that two novel classes of O-linked N-acetylglucosamine oligosaccharide were present. The first series had the structures Galpbeta1-3GlcNAc-ol; Galpbeta1-6(Galpbeta1-3)GlcNAc-ol; and Galpbeta1-2Galpbeta1-6(Galpbeta1-3)GlcNAc-ol, whereas the other series had a 1-4 linkage to N-acetylglucosaminitol and had structures Galpbeta1-4GlcNAc-ol, Galpbeta1-6(Galpbeta1-4)GlcNAc-ol, and Galpbeta1-2Galpbeta1-6(Galpbeta1-4)GlcNAc-ol. We have also investigated the kinetics of in vitro sialylation of these O-linked oligosaccharides by the T. cruzi trans-sialidase and have shown that incorporation of one molecule of sialic acid hinders entry of a second molecule when two potential acceptor sites are present.



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