Send to

Choose Destination
Elife. 2018 Apr 27;7. pii: e32478. doi: 10.7554/eLife.32478.

All-atom molecular dynamics of the HBV capsid reveals insights into biological function and cryo-EM resolution limits.

Author information

Department of Chemistry and Biochemistry, University of Delaware, Newark, United States.
Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, United States.
Department of Physics, University of Illinois at Urbana-Champaign, Urbana, United States.
Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, United States.


The hepatitis B virus capsid represents a promising therapeutic target. Experiments suggest the capsid must be flexible to function; however, capsid structure and dynamics have not been thoroughly characterized in the absence of icosahedral symmetry constraints. Here, all-atom molecular dynamics simulations are leveraged to investigate the capsid without symmetry bias, enabling study of capsid flexibility and its implications for biological function and cryo-EM resolution limits. Simulation results confirm flexibility and reveal a propensity for asymmetric distortion. The capsid's influence on ionic species suggests a mechanism for modulating the display of cellular signals and implicates the capsid's triangular pores as the location of signal exposure. A theoretical image reconstruction performed using simulated conformations indicates how capsid flexibility may limit the resolution of cryo-EM. Overall, the present work provides functional insight beyond what is accessible to experimental methods and raises important considerations regarding asymmetry in structural studies of icosahedral virus capsids.


Cryo-EM resolution; Hepatitis B Virus; Molecular Dynamics Simulation; Single-Particle Image Reconstruction; Virus Capsid; molecular biophysics; none; structural biology

Supplemental Content

Full text links

Icon for eLife Sciences Publications, Ltd Icon for PubMed Central
Loading ...
Support Center