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There are several lectins with anti-H specificity but few of them serve as useful reagents. An anti-H lectin, extracted from the seeds of the plant  Momordica dioica Roxb. ex willd. , was tested for its hemagglutination and inhibition properties, using standard serologic methods and panel RBCs, serum, saliva, milk, and oligosaccharides purified from milk. The extract displayed strongest agglutination with group O RBCs and was weakest with group A 1 B RBCs in a spectrum of O&gt;A 2 &gt;B&gt;A 2 B&gt;A 1 &gt;A 1 B; the extract failed to react with the RBCs from 25 individuals with the Bombay (O h ) phenotype and was inhibited by H secretor saliva, hence it was characterized as anti-H. However, its inhibition by milk samples from five mothers with the Bombay phenotype called into question its specificity as anti-H. The lectin reacted as strongly with group O ii (adult) RBCs as with normal OI RBCs, ruling out its specificity as anti-HI. Hemagglutination inhibition was observed with 2′-fucosyllactose (Type 2 H) and lacto-N-fucopentose-I (Type 1 H), suggesting that the binding of the lectin had preference for H structures. However, inhibition by N-acetyllactosamine, lacto-N-tetraose, and lacto-N-neotetraose suggested that the lectin also recognized unsubstituted terminal beta-linked galactose units. The hemagglutinin property in the present lectin showed an unusual anti-H specificity. The lectin was inhibited by milk from Bombay phenotype individuals and certain milk oligosaccharides not specific for the H antigen.  Immunohematology 2005;21:1–4.

An unusual anti-H lectin inhibited by milk from individuals with the Bombay phenotype