Classical nucleation theory of virus capsids

R. Zandi, P.P.A.M. Schoot, van der, D. Reguera, W.K. Kegel, H. Reiss

Research output: Contribution to journalArticleAcademicpeer-review

153 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)1939-1948
JournalBiophysical Journal
Issue number6
Publication statusPublished - 2006


Dive into the research topics of 'Classical nucleation theory of virus capsids'. Together they form a unique fingerprint.

Cite this