Formation of subviral particles by in vitro translation of subgenomic poliovirus RNAs

• Published in: Journal of general virology Vol. 72; no. 11; pp. 2721 - 2726
• Main Authors: Jore, Jan P. M, Veldhuisen, Gerrit, Pouwels, Peter H, Boeye, Albert, Vrijsen, Raf, Rombaut, Bart
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01.11.1991; Society for General Microbiology
• Subjects: 3C Viral Proteases; Animals; Antigens, Viral - genetics; Antigens, Viral - immunology; Biological and medical sciences; Capsid - genetics; Capsid - immunology; Cell-Free System; Cysteine Endopeptidases - genetics; Cysteine Endopeptidases - immunology; Fundamental and applied biological sciences. Psychology; Microbiology; Morphology, structure, chemical composition, physicochemical properties; poliovirus; Poliovirus - genetics; Poliovirus - immunology; Protein Biosynthesis; Protein Precursors - genetics; Protein Precursors - immunology; Rabbits; RNA, Viral - metabolism; Viral Proteins; Virology; Molecular processing; In vitro translation; RNA; Picornaviridae; Gel electrophoresis; Virus like particle; Enterovirus; Monoclonal antibody; Poliovirus; Virus; Antigen; Sucrose gradient; Molecular assembly; Capsid
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-72-11-2721

1 Medical Biological Laboratory TNO, P.O. Box 45, 2280 AA Rijswijk, The Netherlands and 2 Department of Microbiology and Hygiene, Vrije Universiteit Brussel, Laarbeeklaan 103, B-1090 Brussels, Belgium Rabbit reticulocyte lysates were programmed with either RNA extracted from purified poliovirus or a mixture of mRNAs encoding the capsid precursor, P1, and proteinase 3CD. In both cases, 14S subunits were formed at 30 °C and empty capsids at 37 °C. Both the 14S subunits and empty capsids had the expected polypeptide composition and neutralization epitopes. It is concluded that the proteinase 3CD gene is the only viral genetic information needed for the correct processing of P1 and the formation of 14S subunits, and their assembly into antigenically correct empty capsids. Received 4 April 1991; accepted 25 July 1991.