Competing hydrophobic and screened-Coulomb interactions in hepatitis B virus capsid assembly

被引:135
作者
Kegel, WK
van der Schoot, P
机构
[1] Univ Utrecht, Vant Hoff Lab Phys & Colloid Chem, Debye Res Inst, NL-3584 CH Utrecht, Netherlands
[2] Eindhoven Univ Technol, Eindhoven Polymer Labs, NL-5600 MB Eindhoven, Netherlands
关键词
D O I
10.1529/biophysj.104.040055
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Recent experiments show that, in the range from similar to15 to 45degreesC, an increase in the temperature promotes the spontaneous assembly into capsids of the Escherichia coli-expressed coat proteins of hepatitis B virus. Within that temperature interval, an increase in ionic strength up to five times that of standard physiological conditions also acts to promote capsid assembly. To explain both observations we propose an interaction of mean force between the protein subunits that is the sum of an attractive hydrophobic interaction, driving the self-assembly, and a repulsive electrostatic interaction, opposing the self-assembly. We find that the binding strength of the capsid subunits increases with temperature virtually independently of the ionic strength, and that, at fixed temperature, the binding strength increases with the square root of ionic strength. Both predictions are in quantitative agreement with experiment. We point out the similarities of capsid assembly in general and the micellization of surfactants. Finally we make plausible that electrostatic repulsion between the native core subunits of a large class of virus suppresses the formation in vivo of empty virus capsids, that is, without the presence of the charge-neutralizing nucleic acid.
引用
收藏
页码:3905 / 3913
页数:9
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