The key role of rubella virus glycoproteins in the formation of immune response, and perspectives on their use in the development of new recombinant vaccines.

Rubella is a highly contagious viral disease which is mostly threatens to women of reproductive age. Existent live attenuated vaccines are effective enough, but have some drawbacks and are unusable for a certain group of people, including pregnant women and people with AIDS and other immunodeficiency. Thereby the development of alternative non-replicating, recombinant vaccines undoubtedly is needed. This review discusses the protein E1 and E2 role in formation of immune response and perspectives in development of new generation recombinant vaccines using them.

The role of the 5'-cap structure in viral ribonucleoproteins assembly from potato virus X coat protein and RNAs.

The potato virus X (PVX) virion can be reconstituted in vitro from the virus coat protein (CP) and RNA; heterologous RNAs may be used as well. In our recent study, structure and properties of cognate and heterologous viral ribonucleoproteins (vRNPs) were demonstrated to be similar to those of native virions. The assembly was found to be initiated at the 5' terminus of an RNA and was not dependent on RNA sequence. The aim of the present study was to search for a signal or an essential structural element that directs packaging of viral genetic material into vRNPs. vRNPs were formed by incubation of the PVX CP with heterologous capped RNAs, their functional fragments lacking the cap structure, as well as the capped and uncapped transcripts corresponding to the 5'-terminal region of the genomic PVX RNA. Experimental data show that the presence of the cap structure at the 5' end of a nucleic acid is an important condition for vRNP assembly from RNA and CP. Presumably, the 5'-cap affects conformational state of the RNA region responsible for the efficient interaction with CP and creates conformational encapsidation signal for vRNP assembly.