RNA extracted from highly purified hepatitis A virus (HAV) particles was translated in an RNA-dependent, cell-free reticulocyte lysate system, and the products were analyzed by SDS-polyacrylamide gel electrophoresis and compared with proteins translated from RNA of poliovirus. The efficiency of translation in vitro of HAV RNA was comparable to that of poliovirus RNA. Processing of the putative precursor molecules of HAV proteins, studied in pulse-chase experiments, was impaired when compared with that of poliovirus. By radioimmunoprecipitation it was shown that most proteins produced by translation in vitro were related immunologically to the viral structural proteins of the virion.
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