Equine arteritis virus-induced polypeptide synthesis.

This research investigates the production of virus-specific proteins activated by the equine arteritis virus (EAV). It compares these in-vivo viral proteins with in-vitro end products of EAV RNA translations, and concludes that several proteins may be primary translation products, without needing to be processed from larger precursors.

Outline of the Research

• This research primarily aims to shed light on the synthesis of proteins activated by the equine arteritis virus (EAV).
• To do this, it examines the proteins produced within BHK-21 cells after infection by EAV.
• The examination identifies two major virion proteins – referred to as C and E1 – and other polypeptides of varying molecular weights.

Experimentation Process

• The researchers conducted various experiments, including pulse-chase experiments, which involve monitoring changes in molecules over time, use of amino acid analogues, and protease inhibitors.
• The outcomes of these experiments showed no sign that the viral proteins emerged from larger precursors, suggesting they could be primary translation products.
• The research isolated and translated the six polyadenylated RNAs that appear in EAV-infected cells into an mRNA-dependent reticulocyte cell-free system.

Findings and Conclusion

• The outcome of the RNA6 translation resulted in a product with the molecular weight of the nucleocapsid protein (C).
• EAV genomic RNA was translated into proteins of molecular weight 30,000 and 200,000, while RNA1, the intracellular analogue of genomic RNA, only encoded protein p30.
• The study concludes that the absence of large precursor molecules in infected cells and the findings from the in-vitro translation experiments both imply that some proteins are initial translation products.