PMC:7499584 / 10247-11531 JSONTXT

{"project":"2_test","denotations":[{"id":"32829416-4372604-45163178","span":{"begin":58,"end":62},"obj":"4372604"},{"id":"32829416-1310996-45163179","span":{"begin":1159,"end":1163},"obj":"1310996"},{"id":"32829416-8276811-45163180","span":{"begin":1178,"end":1182},"obj":"8276811"},{"id":"T74623","span":{"begin":58,"end":62},"obj":"4372604"},{"id":"T66993","span":{"begin":1159,"end":1163},"obj":"1310996"},{"id":"T27546","span":{"begin":1178,"end":1182},"obj":"8276811"}],"text":"Following Okayama’s earlier work (1973), Schwartz et al. (1974) showed stimulation of synthesis of free chondroitin sulfate chains by ß-D-xylosides in cultured cells. Esko and Montgomery (1995), following Okayama’s and Schwartz’s earlier work, described xyloside “primers” of glycans that could be employed in tissue culture to prevent sugars from attaching to proteins, proteoglycans and glycolipids. They found ß-D-xylosides initiate glycosaminoglycan (GAG) synthesis by substituting for endogenous xylosylated core proteins. Xylosides will also prime oligosaccharides that resemble glycolipids. N-acetyl-α-D-galactosaminides initiate O-linked oligosaccharide synthesis found on mucins and other glycoproteins and can be used to disrupt O-glycosylation. Disaccharides, (e.g. peracetylated N-acetyllactosaminide), can act as primers. Competing with endogenous substrates, they interdict proteoglycan and glycoprotein glycosylation. Esko used acetylated xylose derivatives where PNP-Xyl treatment decreased heparan sulfate expression on the cell surface of Syndecan 4 cells and abrogated the HCV transmission in a concentration-dependent manner (Shieh et al. 1992; Fritz et al. 1994; Fritz and Esko 2001). Xylosides and thioxylosides should be tested in SARS COV2 infectivity studies."}