N. Gilboa-garber et al., A comparison of the Aplysia lectin anti-I specificity with human anti-I and several other I-detecting lectins, TRANSFUSION, 39(10), 1999, pp. 1060-1064
BACKGROUND: Lectins displaying blood group specificity are important for bl
ood group typing and antigen recognition;Their use in blood banks is especi
ally widespread in situations where there is a shortage of specific antiser
a. This report describes the efficiency of Aplysia gonad lectin as reliable
reagent for the detection of I antigen, which is common on adult human cel
ls but reduced in fetal, newborn, and rare adult red cells.
STUDY DESIGN AND METHODS: The selective hemagglutinating activity of the Ap
lysia lectin was compared with that of human anti-I and several I-reactive
lectins, including two plant lectins, one galactophilic microbial lectin, a
nd 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, di
fferentiating between them and fetal or rare I-negative adult red cells (al
though with less of a difference). In contrast to the plant and microbial l
ectins 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 t
he I-detecting proteins is enhanced at 4 degrees C, but unlike the human an
ti-I Aplysia lectin-induced hemagglutination is stable at room temperature.
CONCLUSIONS: The Aplysia lectin is a reliable anti-I reagent, which strongl
y agglutinates I-positive adult human red cells irrespective of their ABH o
r P system antigens. This lectin is usable at room temperature.