Hemoglobin-specific antibody in a multiply transfused patient with sickle cell disease

• Published in: Blood Vol. 89; no. 6; pp. 2155 - 2158
• Main Authors: NORONHA, P. A, VIDA, L. N, PARK, C. L, HONIG, G. R
• Format: Journal Article
• Language: English
• Published: Washington, DC The Americain Society of Hematology 15.03.1997
• Subjects: Adult; Anemia, Sickle Cell - blood; Anemia, Sickle Cell - immunology; Anemia, Sickle Cell - therapy; Anesthesia. Intensive care medicine. Transfusions. Cell therapy and gene therapy; Antibody Specificity; Binding Sites, Antibody; Biological and medical sciences; Blood. Blood and plasma substitutes. Blood products. Blood cells. Blood typing. Plasmapheresis. Apheresis; Erythrocyte Transfusion - adverse effects; Hemoglobins - immunology; Humans; Isoantibodies - biosynthesis; Isoantibodies - blood; Isoantibodies - chemistry; Male; Medical sciences; Transfusions. Complications. Transfusion reactions. Cell and gene therapy; Human; Hemoglobinopathy; Hemoglobin A; Sickle cell anemia; Multiple; Transfusion; Antibody; Hemopathy; Transfusion reaction; Blood; Genetic disease; Case study; Hemolytic anemia; Treatment; Adult; Complication; Alloimmunization
• ISSN: 0006-4971; 1528-0020
• DOI: 10.1182/blood.V89.6.2155

Human hemoglobins (Hbs) are known to be immunogenic, and both normal and variant forms of Hb have been shown to stimulate antibody formation in a variety of animal species. In patients who are homozygous for the sickle Hb (HbS) mutation, transfusion of normal, HbA-containing erythrocytes provides a potential stimulus for HbA alloimmunization. We tested serum samples for the presence of anti-Hb antibody by a solid-phase enzyme-linked immunosorbent assay (ELISA) using Hb-coated polystyrene microtiter plates. Hb-bound antibody was identified using an antihuman IgG antibody. Serum samples from 89 patients with sickle cell disease were initially tested for evidence of Hb antibody. The serum from three individuals exhibited antibody activity against HbA with little or no activity against HbS. Only one of them, a multiply transfused adult with HbSS, was available for further study. When this patient's antibody was tested against a variety of normal and mutant Hbs using antibody either to human IgG or to kappa chains, the anti-Hb antibody demonstrated specificity for the region of the Hb beta chain corresponding to the site of the amino acid substitution of HbS. The level of activity of the patient's anti-HbA showed no significant change over 1.5 years of observation. The transfusion of erythrocytes containing Hb structurally different from that of the recipient appeared to be capable of stimulating the production of Hb-specific alloimmune antibody.