Membrane association and RNA binding of recombinant hepatitis A virus protein 2C.

Abstract

The direct function of hepatitis A virus (HAV) protein 2C, a putative NTPase, is not known, yet genetic evidence obtained from chimeric viruses carrying the 2C genomic region of different HAV variants indicates that it plays a pivotal role in viral replication. In a first assessment of its potential function(s), membrane and RNA binding properties of HAV 2C were studied after expressing the protein in various recombinant systems. In contrast to poliovirus 2C, expression of HAV 2C was inhibitory to the growth and protein synthesis of bacteria. Deletion of the N-terminal amphipathic helix of 2C abrogated this effect and the ability of 2C to associate with eukaryotic membranes. Both, purified 2C and the N-terminally truncated protein were shown to bind RNA in vitro. Our data taken together suggest that HAV 2C is a multifunctional protein.