A possible role of the viral core protein in the regulation of assembly and disassembly of alphavirus cores.

In many viral systems the genome is part of a stable nucleoprotein complex which has to be dissociated early in infection, in order to make the genome accessible for transcription or translation. It is not directly evident how a nucleoprotein generated as a stable complex during virus assembly can be dissociated during the initial steps of viral multiplication. During analyses of the molecular biology of alphavirus replication it has been shown that the core protein of these viruses is a multifunctional protein. In this manuscript I propose that one of the functions of the core protein, namely its ability to bind to the large subunit of the cellular ribosomes both during synthesis and as a mature protein, allows to regulate the assembly and disassembly of alphavirus cores. I propose that in the early stages of virus infection the core protein is transferred from the core of the incoming virus to the cellular ribosomes, whereas in the late stages of infection when a significant part of the ribosomes contain bound, newly synthesized core protein an efficient transfer of newly synthesized core protein into cores can occur.