1988
DOI: 10.1590/s0074-02761988000500038
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Glycoprotein GP57/51 of Trypanosoma cruzi: structural and conformational epitopes defined with monoclonal antibodies

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Cited by 6 publications
(2 citation statements)
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“…But while there was an apparent difference in the recognition by T cells of separated antigens, none of the specific antigen bands were recognized preferentially by sera of patients with one clinical form vs. another. These studies further describe a glycoprotein component of EPI which migrates diffusely between 57 and 51 kD (GP57/51) (Scharfstein et al, 1986;Murta et al, 1988). GP57/51 antigen is recognized by all patients' sera and cells, and a given patient's PBMC responses to this purified antigen correlate with their responsiveness to crude EPI.…”
Section: Biology Of Trypanosoma Cruzimentioning
confidence: 97%
“…But while there was an apparent difference in the recognition by T cells of separated antigens, none of the specific antigen bands were recognized preferentially by sera of patients with one clinical form vs. another. These studies further describe a glycoprotein component of EPI which migrates diffusely between 57 and 51 kD (GP57/51) (Scharfstein et al, 1986;Murta et al, 1988). GP57/51 antigen is recognized by all patients' sera and cells, and a given patient's PBMC responses to this purified antigen correlate with their responsiveness to crude EPI.…”
Section: Biology Of Trypanosoma Cruzimentioning
confidence: 97%
“…Subcellular localization [9] and proteomics [10] experiments have shown reservosomes to contain large amounts of a cysteine proteinase, known as cruzipain [11] or GP57/51 [12]. The native GP57/51 has been isolated from epimastigotes and used to generate a monoclonal antibody (mAb) [13]. Subcellular localization experiments demonstrated the presence of this protein in vesicles of the endosomal/lysosomal system and close to the flagellar pocket [12, 14].…”
Section: Introductionmentioning
confidence: 99%