Studies on improvement and change of function of hemolytic lectin based on molecular modeling

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In this study, mutants of hemolytic lectin CEL-III were constructed to improve the hemolytic activity and change the Ca-dependency. A fusion protein of earthworm lectin with pore-forming domain of CEL-III was constructed and showed hemagglutinating activity with no Ca-dependency. Furthermore, amino acid residues involved in stacking interaction with carbohydrate in five carbohydrate binding sites of CEL-III were replaced to other amino acids. Among the CEL-III mutants, five mutants (H36F, Y134H, Y181F,Y181W, Y222F) have a stronger hemolytic activity than wild type CEL-III.