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Article
July 1995

Studies in Patients With Corticosteroid Contact Allergy: A Flawed Analysis of Structure-Function Relationships

Author Affiliations

Department of Dermatology State University of New York at Stony Brook Stony Brook, NY 11794-8165

Arch Dermatol. 1995;131(7):851-852. doi:10.1001/archderm.1995.01690190107027
Abstract

The study by Lepoittevin et al1 attempts to analyze the structure-function relationships of allergic contact dermatitis to a panel of steroids. Unfortunately, their analysis is not supported by their data, and their reasoning is oversimplified. T-lymphocytes recognize peptides bound to grooves in major histocompatibility complex molecules (eg, HLA-DR or HLA-A, -B, and -C).2 Haptens are presented bound to these peptides. Thus, the entire antigen consists of a hapten bound to a peptide presented by a major histocompatibility complex molecule. The nature of an antigen is determined by multiple factors: the chemical reactivity of the hapten3; which protein the hapten binds; which amino acid residue the hapten binds4; whether the hapten is conjugated intracellularly or extracellularly; how the protein is processed5; and on which major histocompatibility complex molecule the hapten-peptide complex is presented. Characterization of hapten cross-reactivities solely on the general shape of the hapten ignores

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