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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Publicado: 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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spelling 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
_version_ 1768544818852528128