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A comparison of the Aplysia lectin anti‐I specificity with human anti‐I and several other I‐detecting lectins
Author(s) -
GilboaGarber N.,
Sudakevitz D.,
Levene C.
Publication year - 1999
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1999.39101060.x
Subject(s) - lectin , aplysia , chemistry , biochemistry , biology , neuroscience
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.