Significance N-glycosylation is a common posttranslational modification of extracellular proteins. It plays a role in protein folding in the endoplasmic reticulum and later participates in important protein–carbohydrate interactions. Viruses, in… Click to show full abstract
Significance N-glycosylation is a common posttranslational modification of extracellular proteins. It plays a role in protein folding in the endoplasmic reticulum and later participates in important protein–carbohydrate interactions. Viruses, in particular, are often highly glycosylated. Knowledge of the determinants of modification at a particular site is important for better understanding these processes. One challenge in obtaining this information is separating the effect of the two glycosyltransferases, OST-A and OST-B. Our study focuses on OST-B and reveals how multiple, closely spaced glycosylation sites can influence one another in the context of OST-B glycosylation.
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Year Published: 2022
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