Mutated plant lectin library useful to identify different cells

The 24 nucleotides comprising the carbohydrate-recognition domain of Maacki a amurensis hemagglutinin (MAH) cDNA were randomly mutated. The mutant lect ins were expressed as glutathione-S-transferase fusion proteins in Escheric hia coli and 16 clones were randomly chosen. Although all of 16 recombinant lectins reacted strongly with anti-MAH polyclonal antibody, the carbohydra te-recognition domain of each was unique. As shown by agglutination studies , each mutant MAH lectin was able to bind to erythrocytes from one or more of five animal species in very distinct patterns. Thus, novel plant lectin libraries can be used to discriminate in a highly specific manner among a v ariety of cell types. This technology may prove to be very useful in a numb er of different applications requiring a high level of specificity in cell identification.