dos Reis G A, Maldonado M S, Mendonça-Previato L, Barcinski M A
Infect Immun. 1986 Jan;51(1):369-72. doi: 10.1128/iai.51.1.369-372.1986.
A glycoconjugate (GP-25) was previously purified from Trypanosoma cruzi and shown to be a major immunogenic constituent of the parasite cell surface, capable of inducing specific humoral responses in the vast majority of patients with Chagas' disease. In the present study, the T-cell proliferative response to GP-25 was studied in mice immunized with T. cruzi fractions or whole parasites. Recognition of GP-25 by proliferating T cells requires the participation of syngeneic, accessory spleen cells and is specifically blocked by anti-la antibodies. Furthermore, recognition of GP-25 is influenced by the MHC haplotype of accessory antigen-presenting cells. Short-term, GP-25-specific T-cell lines were used to demonstrate the specificity of anti-GP-25 T cells and to show that this glycoconjugate is not involved in T-cell cross-reactivity with heart antigens. T cells primed with nonpathogenic trypanosomatids are able to recognize the purified T. cruzi GP-25 molecule, indicating that T cells recognize a GP-25 epitope which is shared among trypanosomatids.
一种糖缀合物（GP - 25）先前已从克氏锥虫中纯化出来，并被证明是该寄生虫细胞表面的主要免疫原性成分，能够在绝大多数恰加斯病患者中诱导特异性体液反应。在本研究中，在用克氏锥虫组分或完整寄生虫免疫的小鼠中研究了对GP - 25的T细胞增殖反应。增殖的T细胞对GP - 25的识别需要同基因辅助性脾细胞的参与，并被抗Ia抗体特异性阻断。此外，GP - 25的识别受辅助性抗原呈递细胞的MHC单倍型影响。短期的、GP - 25特异性T细胞系被用于证明抗GP - 25 T细胞的特异性，并表明这种糖缀合物不参与T细胞与心脏抗原的交叉反应。用非致病性锥虫免疫的T细胞能够识别纯化的克氏锥虫GP - 25分子，这表明T细胞识别一种在锥虫中共享的GP - 25表位。
