TY - JOUR
T1 - A comparison of the Aplysia lectin anti-I specificity with human anti-I and several other I-detecting lectins
AU - Gilboa-Garber, Nechama
AU - Sudakevitz, D.
AU - Levene, C.
PY - 1999/10
Y1 - 1999/10
N2 - 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 O(h) 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.
AB - 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 O(h) 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.
UR - http://www.scopus.com/inward/record.url?scp=0032862666&partnerID=8YFLogxK
U2 - 10.1046/j.1537-2995.1999.39101060.x
DO - 10.1046/j.1537-2995.1999.39101060.x
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C2 - 10532598
AN - SCOPUS:0032862666
SN - 0041-1132
VL - 39
SP - 1060
EP - 1064
JO - Transfusion
JF - Transfusion
IS - 10
ER -