Structurally similar woodchuck and human hepadnavirus core proteins have distinctly different temperature dependences of assembly.

ABSTRACT:

Unlabelled

Woodchuck hepatitis virus (WHV), a close relative of human hepatitis B virus (HBV), has been a key model for disease progression and clinical studies. Sequences of the assembly domain of WHV and HBV core proteins (wCp149 and hCp149, respectively) have 65% identity, suggesting similar assembly behaviors. We report a cryo-electron microscopy (cryo-EM) structure of the WHV capsid at nanometer resolution and characterization of wCp149 assembly. At this resolution, the T=4 capsid structures of WHV and HBV are practically identical. In contrast to their structural similarity, wCp149 demonstrates enhanced assembly kinetics and stronger dimer-dimer interactions than hCp149: at 23 °C and at 100 mM ionic strength, the pseudocritical concentrations of assembly of wCp149 and hCp149

SUBMITTER: Kukreja AA 

PROVIDER: S-EPMC4249156 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature