Major Trypanosoma cruzi antigenic determinant in Chagas' heart disease shares homology with the systemic lupus erythematosus ribosomal P protein epitope
A Trypanosoma cruzi λgt11 cDNA clone, JL5, expressed a recombinant protein which was found to react predominantly with chronic Chagas' heart disease sera. The cloned 35-residue-long peptide was identified as the carboxyl-terminal portion of a T. cruzi ribosomal P protein. The JL5 13 carboxyl-te...
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1990
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00951137_v28_n6_p1219_Mesri http://hdl.handle.net/20.500.12110/paper_00951137_v28_n6_p1219_Mesri |
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paper:paper_00951137_v28_n6_p1219_Mesri2023-06-08T15:09:38Z Major Trypanosoma cruzi antigenic determinant in Chagas' heart disease shares homology with the systemic lupus erythematosus ribosomal P protein epitope epitope recombinant protein ribosome protein synthetic peptide adult aged amino acid sequence antigen binding article chagas disease clinical article enzyme linked immunosorbent assay heart disease human priority journal protozoon systemic lupus erythematosus trypanosoma cruzi Amino Acid Sequence Animal Antigens, Protozoan beta-Galactosidase Chagas Cardiomyopathy Comparative Study Enzyme-Linked Immunosorbent Assay Epitopes Human Lupus Erythematosus, Systemic Molecular Sequence Data Phosphoproteins Recombinant Proteins Sequence Homology, Nucleic Acid Support, Non-U.S. Gov't Trypanosoma cruzi Protozoa Trypanosoma Trypanosoma cruzi A Trypanosoma cruzi λgt11 cDNA clone, JL5, expressed a recombinant protein which was found to react predominantly with chronic Chagas' heart disease sera. The cloned 35-residue-long peptide was identified as the carboxyl-terminal portion of a T. cruzi ribosomal P protein. The JL5 13 carboxyl-terminal residues shared a high degree of homology with the systemic lupus erythematosus (SLE) ribosomal P protein epitope. Synthetic peptides comprising the 13 (R-13), 10 (R-10), and 7 (R-7) carboxyl-terminal residues of the JL5 protein were used to study, by enzyme-linked immunosorbent assay, the specificity of the Chagas' disease anti-JL5 and SLE anti-P antibodies. The R-13 peptide defined a linear antigenic determinant of the JL5 recombinant protein. As was proved for JL5, R-13 defined antibody specificities which were significantly increased in chronic Chagas' heart disease patients. Only SLE anti-P positive sera were found to react with JL5 and R-13. Fine epitope mapping showed that Chagas' disease anti-JL5 and SLE anti-P antibodies define similar epitopes within the R-13 peptide. The binding of the SLE sera to JL5 was completely blocked by the R-13 peptide, indicating that the shared specificity between anti-JL5 and anti-P autoantibodies was exclusively limited to the conserved linear epitope(s) within the R-13 peptide. The prevalence of high anti-R-13 antibody titers in Chagas' heart disease patients supports the hypothesis that postulates the existence of autoimmune disorders in Chagas' heart disease. 1990 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00951137_v28_n6_p1219_Mesri http://hdl.handle.net/20.500.12110/paper_00951137_v28_n6_p1219_Mesri |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
epitope recombinant protein ribosome protein synthetic peptide adult aged amino acid sequence antigen binding article chagas disease clinical article enzyme linked immunosorbent assay heart disease human priority journal protozoon systemic lupus erythematosus trypanosoma cruzi Amino Acid Sequence Animal Antigens, Protozoan beta-Galactosidase Chagas Cardiomyopathy Comparative Study Enzyme-Linked Immunosorbent Assay Epitopes Human Lupus Erythematosus, Systemic Molecular Sequence Data Phosphoproteins Recombinant Proteins Sequence Homology, Nucleic Acid Support, Non-U.S. Gov't Trypanosoma cruzi Protozoa Trypanosoma Trypanosoma cruzi |
spellingShingle |
epitope recombinant protein ribosome protein synthetic peptide adult aged amino acid sequence antigen binding article chagas disease clinical article enzyme linked immunosorbent assay heart disease human priority journal protozoon systemic lupus erythematosus trypanosoma cruzi Amino Acid Sequence Animal Antigens, Protozoan beta-Galactosidase Chagas Cardiomyopathy Comparative Study Enzyme-Linked Immunosorbent Assay Epitopes Human Lupus Erythematosus, Systemic Molecular Sequence Data Phosphoproteins Recombinant Proteins Sequence Homology, Nucleic Acid Support, Non-U.S. Gov't Trypanosoma cruzi Protozoa Trypanosoma Trypanosoma cruzi Major Trypanosoma cruzi antigenic determinant in Chagas' heart disease shares homology with the systemic lupus erythematosus ribosomal P protein epitope |
topic_facet |
epitope recombinant protein ribosome protein synthetic peptide adult aged amino acid sequence antigen binding article chagas disease clinical article enzyme linked immunosorbent assay heart disease human priority journal protozoon systemic lupus erythematosus trypanosoma cruzi Amino Acid Sequence Animal Antigens, Protozoan beta-Galactosidase Chagas Cardiomyopathy Comparative Study Enzyme-Linked Immunosorbent Assay Epitopes Human Lupus Erythematosus, Systemic Molecular Sequence Data Phosphoproteins Recombinant Proteins Sequence Homology, Nucleic Acid Support, Non-U.S. Gov't Trypanosoma cruzi Protozoa Trypanosoma Trypanosoma cruzi |
description |
A Trypanosoma cruzi λgt11 cDNA clone, JL5, expressed a recombinant protein which was found to react predominantly with chronic Chagas' heart disease sera. The cloned 35-residue-long peptide was identified as the carboxyl-terminal portion of a T. cruzi ribosomal P protein. The JL5 13 carboxyl-terminal residues shared a high degree of homology with the systemic lupus erythematosus (SLE) ribosomal P protein epitope. Synthetic peptides comprising the 13 (R-13), 10 (R-10), and 7 (R-7) carboxyl-terminal residues of the JL5 protein were used to study, by enzyme-linked immunosorbent assay, the specificity of the Chagas' disease anti-JL5 and SLE anti-P antibodies. The R-13 peptide defined a linear antigenic determinant of the JL5 recombinant protein. As was proved for JL5, R-13 defined antibody specificities which were significantly increased in chronic Chagas' heart disease patients. Only SLE anti-P positive sera were found to react with JL5 and R-13. Fine epitope mapping showed that Chagas' disease anti-JL5 and SLE anti-P antibodies define similar epitopes within the R-13 peptide. The binding of the SLE sera to JL5 was completely blocked by the R-13 peptide, indicating that the shared specificity between anti-JL5 and anti-P autoantibodies was exclusively limited to the conserved linear epitope(s) within the R-13 peptide. The prevalence of high anti-R-13 antibody titers in Chagas' heart disease patients supports the hypothesis that postulates the existence of autoimmune disorders in Chagas' heart disease. |
title |
Major Trypanosoma cruzi antigenic determinant in Chagas' heart disease shares homology with the systemic lupus erythematosus ribosomal P protein epitope |
title_short |
Major Trypanosoma cruzi antigenic determinant in Chagas' heart disease shares homology with the systemic lupus erythematosus ribosomal P protein epitope |
title_full |
Major Trypanosoma cruzi antigenic determinant in Chagas' heart disease shares homology with the systemic lupus erythematosus ribosomal P protein epitope |
title_fullStr |
Major Trypanosoma cruzi antigenic determinant in Chagas' heart disease shares homology with the systemic lupus erythematosus ribosomal P protein epitope |
title_full_unstemmed |
Major Trypanosoma cruzi antigenic determinant in Chagas' heart disease shares homology with the systemic lupus erythematosus ribosomal P protein epitope |
title_sort |
major trypanosoma cruzi antigenic determinant in chagas' heart disease shares homology with the systemic lupus erythematosus ribosomal p protein epitope |
publishDate |
1990 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00951137_v28_n6_p1219_Mesri http://hdl.handle.net/20.500.12110/paper_00951137_v28_n6_p1219_Mesri |
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1768545180430893056 |