PMID:16387781

Citation	Zandi, R, van der Schoot, P, Reguera, D, Kegel, W and Reiss, H (2006) Classical nucleation theory of virus capsids. Biophys. J. 90:1939-48
Abstract	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.
Links	PubMed PMC1386774 Online version:10.1529/biophysj.105.072975
Keywords	Binding Sites; Capsid/chemistry; Capsid/physiology; Capsid Proteins/chemistry; Capsid Proteins/physiology; Computer Simulation; Crystallization/methods; Models, Biological; Models, Chemical; Models, Molecular; Multiprotein Complexes/chemistry; Multiprotein Complexes/physiology; Protein Binding; Virus Assembly/physiology
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