Role of dynamic capsomere supply for viral capsid self-assembly. (30th January 2015)

• Record Type: Journal Article
• Authors: Boettcher, Marvin A; Klein, Heinrich C R; Schwarz, Ulrich S
• Is Part Of: Physical biology. Volume 12:Number 1(2015:Feb.)
• Publication Date: 2015-01-30
• Subjects: viruses -- Brownian dynamics -- protein assembly -- spatial modeling -- patchy particles; 87.10.Mn -- 87.14.E- -- 87.16.dr -- 83.10.Mj; Biophysics -- Periodicals; Biochemistry -- Periodicals; Biology -- Data processing -- Periodicals; 570.5
• DOI: 10.1088/1478-3975/12/1/016014
• Languages: English
• ISSNs: 1478-3967

Abstract

Abstract: Many viruses rely on the self-assembly of their capsids to protect and transport their genomic material. For many viral systems, in particular for human viruses like hepatitis B, adeno or human immunodeficiency virus, that lead to persistent infections, capsomeres are continuously produced in the cytoplasm of the host cell while completed capsids exit the cell for a new round of infection. Here we use coarse-grained Brownian dynamics simulations of a generic patchy particle model to elucidate the role of the dynamic supply of capsomeres for the reversible self-assembly of empty T1 icosahedral virus capsids. We find that for high rates of capsomere influx only a narrow range of bond strengths exists for which a steady state of continuous capsid production is possible. For bond strengths smaller and larger than this optimal value, the reaction volume becomes crowded by small and large intermediates, respectively. For lower rates of capsomere influx a broader range of bond strengths exists for which a steady state of continuous capsid production is established, although now the production rate of capsids is smaller. Thus our simulations suggest that the importance of an optimal bond strength for viral capsid assembly typical for in vitro conditions can be reduced by the dynamic influx of capsomeres in a cellular environment.