Format:
Online-Ressource
Content:
Abstract: Hepatitis B virus (HBV) is an important but difficult to study human pathogen. Most basics of the hepadnaviral life-cycle were unraveled using duck HBV (DHBV) as a model although DHBV has a capsid protein (CP) comprising ~260 rather than ~180 amino acids. Here we present high-resolution structures of several DHBV capsid-like particles (CLPs) determined by electron cryo-microscopy. As for HBV, DHBV CLPs consist of a dimeric α-helical frame-work with protruding spikes at the dimer interface. A fundamental new feature is a ~ 45 amino acid proline-rich extension in each monomer replacing the tip of the spikes in HBV CP. In vitro, folding of the extension takes months, implying a catalyzed process in vivo. DHBc variants lacking a folding-proficient extension produced regular CLPs in bacteria but failed to form stable nucleocapsids in hepatoma cells. We propose that the extension domain acts as a conformational switch with differential response options during viral infection
Note:
eLife. - 9 (2020) , e57277, ISSN: 2050-084X
Language:
English
URN:
urn:nbn:de:bsz:25-freidok-1674338
URL:
https://doi.org/10.7554/eLife.57277
URL:
https://nbn-resolving.org/urn:nbn:de:bsz:25-freidok-1674338
URL:
https://d-nb.info/1219851345/34
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