Production and Characterization of Monoclonal Antibodies Against the Major Cysteine Proteinase of Trypanosoma cruzi
In the present study we describe the production and characterization of a panel of monoclonal antibodies (MoAbs) directed against cruzipain (Crz), the major cysteine proteinase from Trypanosoma cruzi. The five MoAbs, BD6, BF2, CG2, CH8, and DC10 were analysed with respect to affinity and specificity...
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1994
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03009475_v40_n4_p389_GONZALEZ http://hdl.handle.net/20.500.12110/paper_03009475_v40_n4_p389_GONZALEZ |
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paper:paper_03009475_v40_n4_p389_GONZALEZ2023-06-08T15:27:38Z Production and Characterization of Monoclonal Antibodies Against the Major Cysteine Proteinase of Trypanosoma cruzi cruzipain cysteine proteinase monoclonal antibody parasite antigen animal experiment article enzyme activity enzyme linked immunosorbent assay mouse nonhuman trypanosoma cruzi Animal Antibodies, Monoclonal Antibodies, Protozoan Antibody Affinity Antibody Specificity Cysteine Endopeptidases Enzyme-Linked Immunosorbent Assay Epitope Mapping Mice Mice, Inbred BALB C Precipitin Tests Support, Non-U.S. Gov't Trypanosoma cruzi In the present study we describe the production and characterization of a panel of monoclonal antibodies (MoAbs) directed against cruzipain (Crz), the major cysteine proteinase from Trypanosoma cruzi. The five MoAbs, BD6, BF2, CG2, CH8, and DC10 were analysed with respect to affinity and specificity. None of the MoAbs cross‐reacted with papain, which has regions of high homology with Crz. Treatment of the antigen with periodate did not affect the binding of the MoAbs. suggesting that they bind to the polypeptide moiety of Crz. CH8 recognized a continuous epitope located at the C‐terminal extension of the proteinase that appeared to be highly immunogenic. Although the rest of the MoAbs recognized epitopes located in the catalytic domain, the enzymatic activity of Crz was not impaired by the binding of the MoAbs. Characterization of the antibody‐binding sites revealed the presence of at least four separate epitopes. Copyright © 1994, Wiley Blackwell. All rights reserved 1994 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03009475_v40_n4_p389_GONZALEZ http://hdl.handle.net/20.500.12110/paper_03009475_v40_n4_p389_GONZALEZ |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
cruzipain cysteine proteinase monoclonal antibody parasite antigen animal experiment article enzyme activity enzyme linked immunosorbent assay mouse nonhuman trypanosoma cruzi Animal Antibodies, Monoclonal Antibodies, Protozoan Antibody Affinity Antibody Specificity Cysteine Endopeptidases Enzyme-Linked Immunosorbent Assay Epitope Mapping Mice Mice, Inbred BALB C Precipitin Tests Support, Non-U.S. Gov't Trypanosoma cruzi |
spellingShingle |
cruzipain cysteine proteinase monoclonal antibody parasite antigen animal experiment article enzyme activity enzyme linked immunosorbent assay mouse nonhuman trypanosoma cruzi Animal Antibodies, Monoclonal Antibodies, Protozoan Antibody Affinity Antibody Specificity Cysteine Endopeptidases Enzyme-Linked Immunosorbent Assay Epitope Mapping Mice Mice, Inbred BALB C Precipitin Tests Support, Non-U.S. Gov't Trypanosoma cruzi Production and Characterization of Monoclonal Antibodies Against the Major Cysteine Proteinase of Trypanosoma cruzi |
topic_facet |
cruzipain cysteine proteinase monoclonal antibody parasite antigen animal experiment article enzyme activity enzyme linked immunosorbent assay mouse nonhuman trypanosoma cruzi Animal Antibodies, Monoclonal Antibodies, Protozoan Antibody Affinity Antibody Specificity Cysteine Endopeptidases Enzyme-Linked Immunosorbent Assay Epitope Mapping Mice Mice, Inbred BALB C Precipitin Tests Support, Non-U.S. Gov't Trypanosoma cruzi |
description |
In the present study we describe the production and characterization of a panel of monoclonal antibodies (MoAbs) directed against cruzipain (Crz), the major cysteine proteinase from Trypanosoma cruzi. The five MoAbs, BD6, BF2, CG2, CH8, and DC10 were analysed with respect to affinity and specificity. None of the MoAbs cross‐reacted with papain, which has regions of high homology with Crz. Treatment of the antigen with periodate did not affect the binding of the MoAbs. suggesting that they bind to the polypeptide moiety of Crz. CH8 recognized a continuous epitope located at the C‐terminal extension of the proteinase that appeared to be highly immunogenic. Although the rest of the MoAbs recognized epitopes located in the catalytic domain, the enzymatic activity of Crz was not impaired by the binding of the MoAbs. Characterization of the antibody‐binding sites revealed the presence of at least four separate epitopes. Copyright © 1994, Wiley Blackwell. All rights reserved |
title |
Production and Characterization of Monoclonal Antibodies Against the Major Cysteine Proteinase of Trypanosoma cruzi |
title_short |
Production and Characterization of Monoclonal Antibodies Against the Major Cysteine Proteinase of Trypanosoma cruzi |
title_full |
Production and Characterization of Monoclonal Antibodies Against the Major Cysteine Proteinase of Trypanosoma cruzi |
title_fullStr |
Production and Characterization of Monoclonal Antibodies Against the Major Cysteine Proteinase of Trypanosoma cruzi |
title_full_unstemmed |
Production and Characterization of Monoclonal Antibodies Against the Major Cysteine Proteinase of Trypanosoma cruzi |
title_sort |
production and characterization of monoclonal antibodies against the major cysteine proteinase of trypanosoma cruzi |
publishDate |
1994 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03009475_v40_n4_p389_GONZALEZ http://hdl.handle.net/20.500.12110/paper_03009475_v40_n4_p389_GONZALEZ |
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1768544818852528128 |