Generation of class-selective monoclonal antibodies against the penicillin group
| Autor: | Etienne Schacht, Bruno Goddeeris, C. van Dorpe, Patricia Cliquet, Eric Cox |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Lactams
medicine.drug_class Enzyme-Linked Immunosorbent Assay Penicillins Cross Reactions Monoclonal antibody Dicloxacillin Microbiology Mice Antibody Specificity medicine Animals Bovine serum albumin Mice Inbred BALB C biology Chemistry Antibodies Monoclonal General Chemistry Sulfanilamide Carbenicillin Molecular biology Anti-Bacterial Agents Penicillin Monoclonal biology.protein Antibody General Agricultural and Biological Sciences Carrier Proteins medicine.drug |
| Zdroj: | Journal of agricultural and food chemistry. 49(7) |
| ISSN: | 0021-8561 |
| Popis: | To develop a penicillin-specific ELISA, different attempts were made to obtain monoclonal antibodies specific for the common structure of penicillins. Ampicillin was coupled to different carrier proteins (bovine serum albumin, chicken ovalbumin, and thyroglobulin) to render it immunogenic. Different coupling methods were compared: two methods using a cross-linker (glutaraldehyde or a succinimide ester), one carbodiimide-mediated coupling method, and one method without any cross-linker or mediator molecule (physiological binding). Mice were immunized with the conjugates intraperitoneally or in the footpad. A screening ELISA was developed to detect anti-ampicillin antibodies in sera. Specificity and affinity of the antibodies were demonstrated by inhibiting their binding with a 10 mM solution of ampicillin. No difference could be observed using electrofusion or PEG-mediated fusion. For the production of the monoclonals, an intravenous final boost gave antibodies with better specificity and affinity than an intraperitoneal final booster injection. At least one anti-ampicillin monoclonal antibody (19C9) cross-reacts with penicillin G, oxacillin, dicloxacillin, and carbenicillin, and not with sulfanilamide, chloramphenicol, neomycin, and streptomycin, and is therefore considered interesting for developing a penicillin-specific ELISA. |
| Databáze: | OpenAIRE |
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