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• W2113208208 abstract "The addition of N-linked glycans to proteins is normally a cotranslational process that occurs during translocation of the nascent protein to the endoplasmic reticulum. Here, we report on an exception to this rule occurring on the hepatitis B virus (HBV) large L envelope protein that is a subject to co-plus posttranslational N-glycosylation. By using an improved detection system, we identified so far unrecognized, novel isoforms of L. Based on mutational analyses, the use of N-glycosylation inhibitors, and pulse-chase studies, we showed that these isoforms are due to posttranslational N-glycan addition to the asparagines 4 and 112 within the preS domain of L. While an inhibition of N-glycosylation and glycan trimming profoundly blocked virus assembly and release, the posttranslational N-glycosylation of L itself was found to be dispensable for HBV morphogenesis. These data together with previous results implicate that the N-glycosylation requirements of virion release are due to functional inhibition of cell glycoproteins engaged by HBV." @default.
• W2113208208 created "2016-06-24" @default.
• W2113208208 creator A5014850676 @default.
• W2113208208 creator A5064829825 @default.
• W2113208208 date "2007-01-01" @default.
• W2113208208 modified "2023-09-25" @default.
• W2113208208 title "Posttranslational N-glycosylation of the hepatitis B virus large envelope protein" @default.
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• W2113208208 doi "https://doi.org/10.1186/1743-422x-4-45" @default.
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