Protein structure and expression among arenaviruses.

Abstract

The proteins of arenaviruses were first studies by SMADEL and his colleagues (1939, 1940, 1942), with reference to their antigenicity. These workers described the presence of a virus-specific soluble (S) antigen detectable by complement fixation (CF) in homogenates of spleen and lung from LCMV-infected guinea pigs. Soluble antigen could be separated from infectious virus by ultracentrifugation. Repeatedly washed virions reacted poorly in CF tests while the S antigen lost none of its immunoreactivity after ultracentrifugation. These studies were not extended until nearly 3 decades later when Brown and Kirk (1969), Chastel (1970), Simon (1970), and Bro-Jorgensen (1971) described antigens detectable by C F and immunodiffusion in tissues or cell cultures infected with L C M V. Bro-Jorgensen (1971) found two antigenic species by immunodiffusion using infected BHK-21 cells as the antigen source. One antigen was heat stable and resistant to proteolysis, while the second was degraded by both heating and pronase digestion. Both antigens sedimented at a rate of 3.5 S in rate zonal sucrose gradient centrifugation, and based on this S value the molecular weight of the thermolabile S antigen was estimated to be 48 000.