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assembly and disassembly of viral capsids病毒衣壳的装配和拆卸
Journal of Theoretical Medicine, Vol. 6, No. 2, June 2005, 69–72
Assembly and disassembly of viral capsids
ROYA ZANDI†*, DAVID REGUERA†, ROBIJN BRUINSMA‡, WILLIAM GELBART† and JOSEPH RUDNICK‡{
†Department of Chemistry, University of California, Los Angeles, LA 90095, USA
‡Department of Physics, University of California, Los Angeles, LA 90095, USA
We address here a theoretical basis for the icosahedral symmetry that is observed so commonly for viral
capsids, i.e., the single-protein-thick rigid shells that protect the viral genome. In particular, we outline
the phenomenological hamiltonian approach developed recently (see Zandi, R., Reguera, D., Bruinsma,
R., Gelbart, W.M. and Rudnick, J. (2004), Original of icosahedral symmetry in viruses, Proc. Natl.
Acad. Sci. , 101, 15556–15560) to account for the overwhelming prevalence of the Caspar-Klug “T-
number” structures that are found for “spherical” viruses. We feature the role of “conformational
switching energies” defining the competing multimeric states of the protein subunits. The results of
Monte Carlo simulation of this model are argued to shed light as well on the mechanical properties and
genome release mechanism for these viruses.
Keywords: Viral self-assembly; Icosahedral symmetry; Structural transitions; T-number
1. Introduction believed to describe the generic structure of protein
shells.§ However, with current computational capabilities
The cowpea rotic mottle virus (CCMV) is a classical it is neither possible to verify this claim t
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