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

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.

journal_name

Virol J

journal_title

Virology journal

authors

Lambert C,Prange R

doi

10.1186/1743-422X-4-45

subject

Has Abstract

pub_date

2007-05-30 00:00:00

pages

45

issn

1743-422X

pii

1743-422X-4-45

journal_volume

4

pub_type

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