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Classical Nucleation Theory of Virus Capsids

Roya Zandi ^*, Paul van der Schoot , David Reguera , Willem Kegel  and Howard Reiss ^¶

^* Department of Physics, University of California, Riverside, California; Faculteit Technische Natuurkunde, Technische Universiteit Eindhoven, Eindhoven, The Netherlands; Departament de Fisica Fonamental, Universitat de Barcelona, Facultat de Fsica, Barcelona, Spain; Van 't Hoff Laboratorium, Universiteit Utrecht, The Netherlands; and ^¶ Department of Chemistry and Biochemistry, University of California, Los Angeles, California

Correspondence: Address reprint requests to R. Zandi, Tel.: 310-806-1758; E-mail: roya.zandi{at}ucr.edu.

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.

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