ABSTRACT
This chapter describes the application of ion-exchange high-performance liquid chromatography for the purification of viral proteins. Virus proteins are expressed and produced in mainly four systems, bacteria, yeasts, mammalian cells, and insect cells. For purification of structural proteins, virus particles are the preferred starting material. Viral proteins are important as non-structural or structural components of the virion. Structural viral proteins are often tightly associated with either a lipid bilayer envelope or as part of the nucleocapsid. In ion-exchange chromatography, differences in electrostatic interaction between column ligands and charged patches on the proteins are the basis for separation. The main problem encountered in the separation of viral proteins is to maintain complete dissociation of the proteins during the purification procedure. A high reactivity with monoclonal antibodies directed against the intact proteins showed that the conformation of the proteins was not affected by the chromatographic procedure.
