A comparison of the Aplysia lectin anti-I specificity with human anti-I and several other I-detecting lectins

• Published in: Transfusion (Philadelphia, Pa.) Pa.), 1999-10, Vol.39 (10), p.1060-1064
• Main Authors: Gilboa-Garber, N., Sudakevitz, D., Levene, C.
• Format: Article
• Language: English
• Subjects: Adult; AGL = Aplysia gonad lectin; Animals; Antibody Specificity; Biological and medical sciences; Cattle; ECorL = Erythrina corallodendron lectin; Erythrocytes - immunology; Fetal Blood - immunology; Galectins; Hemagglutination Tests; Hemagglutinins - immunology; Hematology; Humans; I Blood-Group System - immunology; Investigative techniques, diagnostic techniques (general aspects); Isoantigens - analysis; Isoantigens - immunology; Lectins - immunology; Medical sciences; PA-IL = Pseudomonas aeruginosa (galactophilic) lectin; Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques; PBS = phosphate-buffered saline; SJL = Sophora japonica lectin; Temperature
• ISSN: 0041-1132; 1537-2995
• DOI: 10.1046/j.1537-2995.1999.39101060.x

BACKGROUND: Lectins displaying blood group specificity are important for blood group typing and antigen recognition. Their use in blood banks is especially widespread in situations where there is a shortage of specific antisera. This report describes the efficiency of Aplysia gonad lectin as a reliable reagent for the detection of I antigen, which is common on adult human cells but reduced in fetal, newborn, and rare adult red cells. STUDY DESIGN AND METHODS: The selective hemagglutinating activity of the Aplysia lectin was compared with that of human anti‐I and several I‐reactive lectins, including two plant lectins, one galactophilic microbial lectin, and bovine spleen galectin. RESULTS: The comparison has revealed that Aplysia gonad lectin, like human anti‐I, strongly agglutinates and adsorbs to adult I‐positive red cells, differentiating between them and fetal or rare I‐negative adult red cells (although with less of a difference). In contrast to the plant and microbial lectins examined, its I‐affinity does not depend on the presence of ABH or P system antigens and it clearly detects higher I antigen expression in Oh red cells. The hemagglutinating activity of Aplysia lectin as that of all the I‐detecting proteins is enhanced at 4°C, but unlike the human anti‐I Aplysia lectin‐induced hemagglutination is stable at room temperature. CONCLUSIONS: The Aplysia lectin is a reliable anti‐I reagent, which strongly agglutinates I‐positive adult human red cells irrespective of their ABH or P system antigens. This lectin is usable at room temperature.