cefoxitin and globotetraose

Lectins have been used at length for basic research and clinical applications. New insights into the molecular recognition properties enhance our basic understanding of carbohydrate-protein interactions and aid in the design/development of new lectins. In this study, we used a combination of cell-based assays, glycan microarrays, and X-ray crystallography to evaluate the structure and function of the recombinant Bauhinia forficata lectin (BfL). The lectin was shown to be cytostatic for several cancer cell lines included in the NCI-60 panel; in particular, it inhibited growth of melanoma cancer cells (LOX IMVI) by over 95%. BfL is dimeric in solution and highly specific for binding of oligosaccharides and glycopeptides with terminal N-acetylgalactosamine (GalNAc). BfL was found to have especially strong binding (apparent K. Structural data are available in the PDB under the accession numbers 5T50, 5T52, 5T55, 5T54, 5T5L, 5T5J, 5T5P, and 5T5O.

Topics: Acetylgalactosamine; Antigens, Tumor-Associated, Carbohydrate; Antineoplastic Agents, Phytogenic; Bauhinia; Binding Sites; Blood Group Antigens; Cell Line, Tumor; Cloning, Molecular; Crystallography, X-Ray; Dimerization; Escherichia coli; Gene Expression; Globosides; Glycopeptides; Humans; Hydrogen Bonding; Kinetics; Models, Molecular; Oligosaccharides; Plant Extracts; Plant Lectins; Protein Binding; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Recombinant Proteins; Substrate Specificity