The first example of a paraben-dependent antibody to an Rh protein

• Published in: Transfusion (Philadelphia, Pa.) Vol. 41; no. 3; pp. 371 - 374
• Main Authors: Judd, W. John, Storry, Jill R., Annesley, Thomas D., Reid, Marion E., Bensette, Michelle, Waddington, Sherry, Dake, LouAnn, Rohrkemper, David, Valdez, Ricardo
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Science Inc 01.03.2001; Blackwell Publishing
• Subjects: Adult; Anesthesia. Intensive care medicine. Transfusions. Cell therapy and gene therapy; Biological and medical sciences; Blood. Blood and plasma substitutes. Blood products. Blood cells. Blood typing. Plasmapheresis. Apheresis; C-LISS = commercial LISS; Erythrocytes - immunology; Female; Humans; Isoantibodies - analysis; Kidd Blood-Group System - immunology; Medical sciences; Parabens - adverse effects; Parabens - chemistry; Pregnancy; Rho(D) Immune Globulin - immunology; Transfusions. Complications. Transfusion reactions. Cell and gene therapy; UMHS = University of Michigan Health Systems; Benzoic acid; Case study; Human; Hematology; Antibody; Female; Rh-System
• ISSN: 0041-1132; 1537-2995
• DOI: 10.1046/j.1537-2995.2001.41030371.x

BACKGROUND: Parabens are added to a commercial LISS (C‐LISS) to retard microbial growth. Paraben‐dependent anti‐Jka has been detected by the use of C‐LISS. CASE REPORT: Serum from a D+ woman reacted in antiglobulin tests with RBCs stored (2‐4 hours, 22‐25°C) in C‐LISS (Löw and Messeter formulation, Immucor). Freshly prepared C‐LISS‐suspended RBCs did not react; nor did RBCs stored in LISS‐additive reagents, PEG, saline, or homemade LISS. RESULTS: Studies using C‐LISS‐stored RBCs revealed an antibody that reacted with D+ and rrV+ RBCs, but not with r′r, r′′r, or rrV‐VS‐ RBCs. All partial D RBC phenotypes tested reacted, as did D+LW‐, rGr, r′′Gr, ryr, r′srV+VS+, and r′srV‐VS+ RBCs. The active ingredient in C‐LISS was propylparaben. Other LISS ingredients were not required; saline solutions of propylparaben, ethylparaben, methyl salicylate, 2‐phenoxyethanol, and butylparaben were active. Methylparaben and methyl‐m‐hydroxybenzoate were inactive. Reactivity to C‐LISS‐stored RBCs could not be inhibited by propylparaben. Reactivity with D+V‐ and D‐V+VS+ RBCs was not separable by adsorption‐elution. CONCLUSIONS: This antibody likely detects a neoantigen formed between active compounds and RBC membranes. Review of the structure of active compounds suggests that proximity between methyl and hydroxyl groups is important for binding with RBC membranes. The role of RhD is unclear; no single portion of RhD protein appears to be implicated.