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 degrees 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.
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 degrees 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.