6533b837fe1ef96bd12a2061

RESEARCH PRODUCT

Posttranslational N-glycosylation of the hepatitis B virus large envelope protein

Carsten LambertReinhild Prange

subject

Gene Expression Regulation ViralHepatitis B virusGlycosylationGlycosylationViral transformationBiologymedicine.disease_causeHepatitis B virus PRE betaCell Linelcsh:Infectious and parasitic diseaseschemistry.chemical_compoundViral Envelope ProteinsN-linked glycosylationViral entryVirologymedicineHumansProtein Isoformslcsh:RC109-216Hepatitis B viruschemistry.chemical_classificationResearchEndoplasmic reticulumEpithelial CellsVirologyProtein Structure TertiaryCell biologycarbohydrates (lipids)Infectious DiseaseschemistryGlycoproteinProtein Processing Post-Translational

description

Abstract Background 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. Results 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. Conclusion 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.

yearjournalcountryeditionlanguage
2007-03-22Virology Journal
https://doi.org/10.1186/1743-422x-4-45