Proceedings of the National Academy of Sciences · 1989 · 10 citations · 21 references
Life SciencesImmunologyAdaptive ImmunityClinical ImmunologyVaccine ImmunologyAntibody CharacterizationAntibody-antigen RecognitionAntibody-mediated ProtectionAntibody-mediated Toxin NeutralizationCell-surface Protein LabelingDiphtheria ToxinSurface Protein DegradationToxin AntigenicityToxin Internalization
An anti-idiotypic serum prepared against the combining site (idiotype) of specific anti-diphtheria toxoid antibodies was characterized with respect to its interaction with highly diphtheria toxin-sensitive Vero cells. Although the anti-idiotypic serum protected Vero cells against the cytotoxic action of diphtheria toxin, it did not prevent the binding of 125I-labeled diphtheria toxin to the cells but did inhibit the internalization and degradation of 125I-labeled toxin. This anti-idiotypic serum immunoprecipitated a cell-surface protein from radiolabeled Vero cells with an apparent Mr of approximately 15,000. These results are consistent with the hypothesis that the anti-idiotypic serum contains antibodies that carry an internal image of an internalization site on the toxin and that a cell-surface protein involved in toxin internalization possesses a complementary site recognized by both the toxin and the anti-idiotypic antibodies.
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Alain B. Schreiber, Pierre Olivier Couraud, Carl André et al. · Proceedings of the National Academy of Sciences · 1980 · 173 citations · Full text
Pharmacy, Immunology, Pharmacology +15