Identification of a molecular code embedded in protein for regulating its glycosylation. Many proteins in nature exist as glycoproteins, which are molecules comprised of protein (polypeptide chain) and glycan (sugar chain). While the protein structure is determined on the basis of its genetic bluep
Specific 29-amino-acid sequence from LAMP-1 serves as a “Lewis X code,” which is deciphered by FUT9, and it can be embedded into erythropoietin to evoke Lewis X modification. Credit: Nagoya City University Graduate School of Pharmaceutical SciencesMany proteins in nature exist as glycoproteins, which are molecules comprised of protein and glycan . While the protein structure is determined on the basis of its genetic blueprint, the information on glycans is not directly encoded by the genome.
Most biopharmaceuticals are actually glycoproteins, as best exemplified by therapeutic antibodies. Their glycan structures are critical for their efficacy and safety. Therefore, the control of glycosylation is an important issue in the development of biopharmaceuticals. Their findings on a regulatory code of protein glycosylation are expected to pave the way for controlling glycosylation of biopharmaceuticals.
Reference: “An embeddable molecular code for Lewis X modification through interaction with fucosyltransferase 9” 13 July 2022,
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