Recombinant Prokaryotic Lectins

More than 50% of proteins are glycosylated and glycans are known to mediate a wide range of biological processes, often through interactions with specific carbohydrate binding proteins called lectins. Changes in the glycosylation patterns of biomolecules and cells are now known to be associated with many diseases and this presents opportunities for the development of novel diagnostic approaches. Consequently there has been an explosion of interest in the field of glycobiology and a demand for effective tools enabling sensitive detection, isolation and analysis of glycosylated biomolecules. In addition, many biopharmaceuticals are glycosylated molecules and inappropriate glycosylation can significantly impact their clinical efficacy and immunogenicity. Glycoselective tools enabling simple, rapid and sensitive analysis of biotherapeutics would increase the efficiency of both biotherapeutic development and manufacturing thereby reducing the costs. Scalable technologies enabling the selective purification of optimally glycosylated products would help producers meet regulatory requirements and help deliver safer, more effective products to patients.These RPLs present new opportunities to develop enhanced glycoselective tools for glycoprotein analysis and scalable selective purification overcoming the limitations that restricted the utility of plant lectins.