Mutated plant lectin library useful to identify different cells.
The 24 nucleotides comprising the carbohydrate-recognition domain of Maackia amurensis hemagglutinin (MAH) cDNA were randomly mutated. The mutant lectins were expressed as glutathione-S-transferase fusion proteins in Escherichia coli and 16 clones were randomly chosen. Although all of 16 recombinant lectins reacted strongly with anti-MAH polyclonal antibody, the carbohydrate-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 variety of cell types. This technology may prove to be very useful in a number of different applications requiring a high level of specificity in cell identification.
Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
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D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D017931:DNA Primers; D006386:Hemagglutination Tests; D016297:Mutagenesis, Site-Directed; D010835:Phytohemagglutinins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D017931:DNA Primers; D010835:Phytohemagglutinins; C100156:leukoagglutinins, plants