Reference: “An embeddable molecular code for Lewis X modification through interaction with fucosyltransferase 9” 13 July 2022, Communications Biology.DOI: 10.1038/ s42003-022-03616-1.
Funding: Japan Science and Technology Agency, Grants-in-Aid for Scientific Research.
Under these circumstances, a collaborative research study group, including scientists at Nagoya City University, National Institutes of Natural Sciences, and Academia Sinica, has discovered a specific amino acid sequence in a polypeptide that induces a specific glycan structure called Lewis X.
The group of researchers in Japan has actually formerly shown that Lewis X specifically customizes the protein LAMP-1 in mouse neural stem cells through the enzymatic action of fucosyltransferase 9 (FUT9). They likewise discovered that a series consisting of 29-amino-acid residues in LAMP-1 promotes Lewis X modification catalyzed by the enzyme, and this sequence induces Lewis X adjustment when merged to other proteins utilized as biopharmaceuticals.
By Nagoya City University
July 13, 2022
Specific 29-amino-acid sequence from LAMP-1 acts as a “Lewis X code,” which is deciphered by FUT9, and it can be embedded into erythropoietin to evoke Lewis X adjustment. Credit: Nagoya City University Graduate School of Pharmaceutical Sciences
Recognition of a molecular code embedded in protein for managing its glycosylation.
Numerous proteins in nature exist as glycoproteins, which are molecules comprised of protein (polypeptide chain) and glycan (sugar chain). Under these circumstances, a collaborative research study group, consisting of scientists at Nagoya City University, National Institutes of Natural Sciences, and Academia Sinica, has actually found a specific amino acid series in a polypeptide that induces a specific glycan structure called Lewis X.
The group of scientists in Japan has previously revealed that Lewis X particularly customizes the protein LAMP-1 in mouse neural stem cells through the enzymatic action of fucosyltransferase 9 (FUT9). They also found that a sequence consisting of 29-amino-acid residues in LAMP-1 promotes Lewis X modification catalyzed by the enzyme, and this sequence causes Lewis X modification when merged to other proteins utilized as biopharmaceuticals.
The control of glycosylation is a crucial concern in the development of biopharmaceuticals. Their findings on a regulative code of protein glycosylation are anticipated to pave the way for managing glycosylation of biopharmaceuticals.
