Mhv. Boas et al., REACTIVITY OF CHAGASIC SERA WITH CRUDE AND HIGHLY PURIFIED GLYCOSPHINGOLIPID FRACTIONS FROM TRYPANOSOMA-CRUZI EPIMASTIGOTES, Journal of clinical laboratory analysis, 8(5), 1994, pp. 260-266
The reactivities of sera from patients with Chagas disease or from T.
cruzi-immunized rabbits with two different lipid preparations of T. cr
uziwere assessed using epimastigote antigens. Serum reactivities were
determined using a quantitative enzyme-linked immunosorbent assay (ELI
SA). Antigen 1 represents the lower phase obtained from crude lipid ex
tract after Folch partition (LCL). Antigen 2 is a highly purified glyc
osphingolipid fraction (GSL). The LCL antigen discriminated quite well
the reactivities of Chagasic patients' sera and sera from healthy ind
ividuals, as well as between the serum from a T. cruzi-immunized rabbi
t (TIRS) and normal rabbit serum (NRS). A strong reactivity with GSL w
as obtained with TIRS. Reactivity with GSL was also obtained with huma
n Chagasic sera. Compared to a group of normal individuals, the reacti
ons of antibodies directed against lipid antigens were considerably in
creased in sera of patients with Chagas disease. Chagasic sera did not
differentiate between glycolipids with terminal beta-glucosyl or beta
-galactosyl nonreducing units. They discriminated, however, glucosylce
ramides with differences in the ceramide structure. To determine the s
pecificity of Chagasic sera, antibodies isolated on LCL-immunosorbent
(LCL-Ch Abs) as well as on laminin-immunosorbent (Lam-Ch Abs) were tes
ted against laminin and LCL antigens. We found that Lam-Ch Abs reacted
with murine laminin, whereas the reaction was negative with LCL. In c
ontrast, the LCL-Ch Abs reacted either with LCL antigens or with lamin
in. The reactivity with laminin was strong in comparison with LCL. Res
ults suggest that although the glycolipids are recognized by Chagasic
patients' sera, the reactive antibodies are not specific since they re
acted quite well with murine laminin. Polyspecific antibodies from Cha
gasic sera have already been described using other unrelated antigens.
(C) 1994 Wiley-Liss, Inc.