Production and Characterization of Monoclonal Antibodies Against the Major Cysteine Proteinase of Trypanosoma cruzi
| Autor: | G. Gonzalez, Anders Örn, K.‐O. Grönvik, J. J. Cazzulo |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
medicine.drug_class
Trypanosoma cruzi Immunology Antibody Affinity Protozoan Proteins Antibodies Protozoan Enzyme-Linked Immunosorbent Assay Cruzipain Monoclonal antibody Epitope Mice chemistry.chemical_compound Antigen Antibody Specificity medicine Animals chemistry.chemical_classification Mice Inbred BALB C biology Antibodies Monoclonal General Medicine biology.organism_classification Precipitin Tests Molecular biology Cysteine Endopeptidases Papain Enzyme chemistry Biochemistry Epitope Mapping Cysteine |
| Zdroj: | Scandinavian Journal of Immunology. 40:389-394 |
| ISSN: | 1365-3083 0300-9475 |
| DOI: | 10.1111/j.1365-3083.1994.tb03479.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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