Characterization of anti-idiotype reagents to bovine herpesvirus-1 monoclonal antibody
| Autor: | J.L. Morrill, D.J. Orten, Frank Blecha, H.C. Minocha |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
medicine.drug_class
animal diseases viruses Immunology Enzyme-Linked Immunosorbent Assay Antibodies Viral Monoclonal antibody Epitope Epitopes Immunoglobulin Fab Fragments Mice Viral Proteins Immunoglobulin Idiotypes Affinity chromatography Pepsin Neutralization Tests medicine Animals Antigens Viral Herpesvirus 1 Bovine Viral Structural Proteins chemistry.chemical_classification Mice Inbred BALB C General Veterinary biology Antibodies Monoclonal biochemical phenomena metabolism and nutrition biology.organism_classification Molecular biology Bovine herpesvirus 1 Antibodies Anti-Idiotypic chemistry Immunoglobulin G Reagent biology.protein Rabbits Antibody Glycoprotein |
| Zdroj: | Veterinary Immunology and Immunopathology. 20:1-14 |
| ISSN: | 0165-2427 |
| Popis: | A monoclonal antibody (MAb) to a neutralization epitope on the 97-kD glycoprotein of bovine herpesvirus-1 (BHV-1) was used to prepare an anti-idiotypic antibody in rabbits. Purified F(ab')2 fragments of the MAb were used to immunize the animals and the sera containing the greatest anti-idiotype activity were identified by ELISA. After digestion of the immunoglobulins with pepsin and purification by affinity chromatography, anti-idiotype F(ab')2 fragments reacted specifically with the MAb in ELISA. Binding of the anti-idiotypic (anti-id) antibody was inhibited by preincubation of the MAb with BHV-1. Using an ELISA inhibition assay with BHV-1, the anti-id reagent inhibited the binding of anti-BHV-1 MAb to BHV-1, suggesting that the anti-id mimics an epitope of the 97-kD glycoprotein by binding the antigen combining site of the MAb. Development and characterization of this anti-id and future studies of its immunomodulatory effects are discussed. |
| Databáze: | OpenAIRE |
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