Characterization of monoclonal antibodies to heat-labile enterotoxin encoded by a plasmid from a clinical isolate of Escherichia coli
| Autor: | Randall K. Holmes, B W Belisle, E M Twiddy |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
medicine.drug_class
Bacterial Toxins Immunology Enterotoxin Cross Reactions Heat-labile enterotoxin medicine.disease_cause Monoclonal antibody Microbiology Epitope Enterotoxins Mice Antigen Neutralization Tests Escherichia coli medicine Animals Humans Escherichia coli Infections Mice Inbred BALB C Hybridomas biology Escherichia coli Proteins Cholera toxin Antibodies Monoclonal Antibodies Bacterial Molecular biology Infectious Diseases Immunoglobulin M Immunoglobulin G biology.protein Parasitology Binding Sites Antibody Antibody Research Article Plasmids |
| Zdroj: | Infection and Immunity. 43:1027-1032 |
| ISSN: | 1098-5522 0019-9567 |
| Popis: | Eight selected hybridoma cell lines that produced monoclonal antibodies against heat-labile enterotoxin from an Escherichia coli strain of human origin (LTh) were characterized. Antibodies produced by these cell lines were tested for binding specificity in a series of solid-phase radioimmunoassays and Western blots by using as test antigens LTh, the A, A1, A2, and B polypeptides of LTh, the heat-labile enterotoxin from an E. coli strain of porcine origin, and cholera toxin. The monoclonal antibodies were also tested for isotype and ability to neutralize LTh. Two of the anti-LTh monoclonal antibodies cross-reacted with cholera toxin, and six were specific for determinants of LTh that were not present on cholera toxin. One was specific for a unique epitope of LTh that was not shared by the heat-labile enterotoxin from an E. coli strain of porcine origin or cholera toxin. Four antibodies specific for epitopes on the B subunit of LTh (LTh-B) reacted with pentameric LTh-B but did not react in Western blots with monomeric LTh-B. The remaining four antibodies were specific for epitopes on LTh-A; two of these antibodies bound to A1, one reacted with A2, and one recognized only intact LTh-A. Only one monoclonal antibody had detectable neutralizing activity, and it was specific for LTh-A. |
| Databáze: | OpenAIRE |
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