High plasticity of the hepatitis B virus capsid revealed by conformational stress.
Hepatitis B virus (HBV) replicates through reverse transcription inside its icosahedral nucleocapsid. The internal genome status is signaled to the capsid surface, predicting regulated conformational changes in the capsid structure. To probe their nature and extent, we imposed local conformational stress on the outer surface of HBV capsid-like particles, and monitored its consequences by electron cryomicroscopy and image reconstruction. The capsid structure had an enormous flexibility and robustness as a whole, as well as within the subunits, whose spikes were able to rotate by as much as 40 degrees against the distal interdimer contact sites. The likely hinge for the swiveling movement was the conserved Gly111 residue at the inner surface of the capsid. The stress imposed from the outside also affected the internal capsid organization, implying a specific route for the flow of conformational information between capsid interior and exterior as required for signaling of the genome status.
Böttcher
Bettina
B
European Molecular Biology Laboratory, Meyerhofstr. 1, D-69117 Heidelberg, and University Hospital Freiburg Internal Medicine II/Molecular Biology, Germany. boettcher@embl-heidelberg.de
Vogel
Maren
M
Ploss
Martin
M
Nassal
Michael
M
D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry* / Q000648:ultrastructure; D036022:Capsid Proteins / Q000737:chemistry / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D017930:Genes, Reporter; D005998:Glycine / Q000737:chemistry; D006515:Hepatitis B virus / Q000737:chemistry* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D011392:Proline / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D036022:Capsid Proteins; D011392:Proline; D005998:Glycine