Classical nucleation theory of virus capsids.
A fundamental step in the replication of a viral particle is the self-assembly of its rigid shell (capsid) from its constituent proteins. Capsids play a vital role in genome replication and intercellular movement of viruses, and as such, understanding viral assembly has great potential in the development of new antiviral therapies and a systematic treatment of viral infection. In this article, we assume that nucleation is the underlying mechanism for self-assembly and combine the theoretical methods of the physics of equilibrium polymerization with those of the classical nucleation to develop a theory for the kinetics of virus self-assembly. We find expressions for the size of the critical capsid, the lag time, and the steady-state nucleation rate of capsids, and how they depend on both protein concentration and binding energy. The latter is a function of the acidity of the solution, the ionic strength, and the temperature, explaining why capsid nucleation is a sensitive function of the ambient conditions.
Zandi
Roya
R
Department of Physics, University of California, Riverside, California, USA. zandi@ucr.edu
van der Schoot
Paul
P
Reguera
David
D
Kegel
Willem
W
Reiss
Howard
H
D001665:Binding Sites; D002213:Capsid / Q000737:chemistry* / Q000502:physiology*; D036022:Capsid Proteins / Q000737:chemistry* / Q000502:physiology*; D003198:Computer Simulation; D003460:Crystallization / Q000379:methods; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry / Q000502:physiology; D011485:Protein Binding; D019065:Virus Assembly / Q000502:physiology*
D036022:Capsid Proteins; D046912:Multiprotein Complexes