N-linked glycosylation of hepatitis B surface antigens is involved but not essential in the assembly of hepatitis delta virus

Chuan Jen Wang, Shian Ying Sung, Ding Shinn Chen, Pei Jer Chen

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20 引文 斯高帕斯(Scopus)

摘要

Hepatitis delta virus (HDV) is a defective virus requiring the hepatitis B virus (HBV) to provide hepatitis B surface antigens as the envelope protein. The hepatitis B surface antigens are posttranslationally modified by N-linked glycosylation, and its significance in HDV assembly was investigated with a cotransfection system using human hepatoma cell line Huh-7. After the N-linked glycosylation of HBsAg was blocked by tunicamycin treatment, the packaging of HDV in the culture system could be suppressed to a level as low as 5-10% of the untreated control. The extent of inhibition correlated with the increased concentrations of tunicamycin. In contrast, the loss of HBsAg glycosylation did not affect the efficiency of assembly of HBV particles. When the N-linked glycosylation site of small HBsAg at amino acid 146 was mutated from asparagine to glutamine, the mutant HBsAg packaged only a modest amount of HDV particles. The quantity and kinetics of formation of HDV particles in culture system were reduced by the depletion of HBsAg glycosylation. Therefore HDV, similar to influenza and vesicular stomatitis viruses, depends on glycosylation of the envelope proteins as a signal for envelope protein maturation and for virion formation.
原文英語
頁(從 - 到)28-36
頁數9
期刊Virology
220
發行號1
DOIs
出版狀態已發佈 - 六月 1 1996
對外發佈Yes

ASJC Scopus subject areas

  • Medicine(all)
  • Virology

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