engleski

Interactions governing virus self-assembly

I will present recent investigations of interactions governing virus self-assembly [1, 2, 3, 4]. It is known that proteins and nucleic acids comprising viruses carry a large charge in the solution. Thus, the electrostatic interactions that are screened by the salt in the physiological conditions should be of importance for the virus self-assembly. It has been demonstrated that the electrostatic interactions in combination with entropic and self-repulsion interactions acting within a nucleic polyelectrolyte molecule (genome) impose strong limits on viral composition that can be achieved by spontaneous assembly [2]. This means that salt concentration, charge on viral proteins and the length of the genome determine whether the assembly proceeds spontaneously or not, i.e. whether the functional virus is a thermodynamical (free energy) minimum of the problem [2, 3]. I shall also present recent results on the formation of „chimeral“ viruses, containing the virus proteins (capsid, coating) of the wild-type viruses, but functionalized charged nanospheres instead of their genome molecules [4]. [1] A. Šiber and R. Podgornik, "Role of electrostatic interactions in the assembly of empty spherical viral capsids", Phys. Rev. E 76, 061906 (2007). [2] A. Šiber and R. Podgornik, "Nonspecific interactions in spontaneous assembly of empty versus functional single-stranded RNA viruses“, Phys. Rev. E 78, 051915 (2008). [3] A. Šiber and A. Majdandžić, "Spontaneous curvature as a regulator of the size of virus capsids“, Phys. Rev. E 80, 021910 (2009). [4] A. Šiber, R. Zandi and R. Podgornik, "Thermodynamics of nanospheres encapsulated in virus capsids“, Phys. Rev. E 81, 051919 (2010).

virus; interactions; electrostatics; protein

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