Abstract
The variety of chemically diverse pharmacologically-active compounds administered to patients is large and seemingly forever growing, and, with every new drug released and administered, there is always the potential of an allergic reaction. The most commonly occurring allergic responses to drugs are the type I, or immediate hypersensitivity reactions mediated by IgE antibodies. These reactions may affect a single organ, such as the nasopharynx (allergic rhinitis), eyes (conjunctivitis), mucosa of mouth/throat/tongue (angioedema), bronchopulmonary tissue (asthma), gastrointestinal tract (gastroenteritis) and skin (urticaria, eczema), or multiple organs (anaphylaxis), causing symptoms ranging from minor itching and inflammation to death. It seems that almost every drug is capable of causing an immediate reaction and it is unusual to find a drug that has not provoked an anaphylactic response in at least one patient. These facts alone indicate the extraordinary breadth of recognition of IgE antibodies for drugs ranging from relatively simple structures, for example, aspirin, to complex molecules, such as the macrolide antibiotics composed of a large macrocyclic ring with attached deoxy sugars. This wide recognition profile is borne out at the molecular level by results of quantitative immunochemical studies where hapten inhibition investigations have identified structural determinants complementary to IgE antibodies in the sera of allergic subjects. Allergenic determinants have been identified on a variety of drugs including neuromuscular blockers, penicillins, cephalosporins, opioids, thiopentone, sulfonamides, trimethoprim, quinolones, chlorhexidine and the non-steroidal anti-inflammatory drug aspirin. It is already clear that IgE can distinguish fine structural differences on a wide variety of molecules, determinants may be at least as small as an amino group or encompass the whole molecule, and individual drugs may demonstrate allergenic heterogeneity.
Highlights
IgE Antibody Recognition of DrugsFrom the foundation years of the science of immunology, a prime requirement for a substance to exhibit immunogenicity, that is to act as an antigen, was said to be the inherent property of a certain minimum size
We examine IgE antibody responses in immediate, type I hypersensitivities to a range of different drugs together with findings so far on the specificities of the antibody combining site-drug allergenic determinants interactions
The results were similar to earlier quantitative inhibition findings employing an immunoassay for cephalosporin-reactive IgE in the sera of patients allergic to cephalothin [20] and further suggested that as well as the methylene structure, the thiophene ring acts as a bioisostere of the benzene ring in the side chain of benzylpenicillin [19]
Summary
From the foundation years of the science of immunology, a prime requirement for a substance to exhibit immunogenicity, that is to act as an antigen, was said to be the inherent property of a certain minimum size. Following Landsteiner's early demonstrations that simple chemicals such as acyl chlorides and acid anhydrides could be made antigenic by coupling these haptens to a suitable carrier protein (for example albumins) [2], it was found that employment of certain adjuvants and immunization schedules sometimes elicited good antibody responses to so-called ‘small’ peptides (
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