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Classical nucleation theory of virus capsids.

Authors :
Zandi R
van der Schoot P
Reguera D
Kegel W
Reiss H
Source :
Biophysical journal [Biophys J] 2006 Mar 15; Vol. 90 (6), pp. 1939-48. Date of Electronic Publication: 2005 Dec 30.
Publication Year :
2006

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.

Details

Language :
English
ISSN :
0006-3495
Volume :
90
Issue :
6
Database :
MEDLINE
Journal :
Biophysical journal
Publication Type :
Academic Journal
Accession number :
16387781
Full Text :
https://doi.org/10.1529/biophysj.105.072975