Primary structure and gene organization of human hepatitis A virus.
- 1 May 1985
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 82 (9) , 2627-2631
- https://doi.org/10.1073/pnas.82.9.2627
Abstract
The RNA genome of human hepatitis A virus (HAV) was molecularly cloned. Recombinant DNA clones representing the entire HAV RNA were used to determine the primary structure of the viral genome. The length of the viral genome is 7478 nucleotides. An open reading frame starting at nucleotide 734 and terminating at nucleotide 7415 encodes a polyprotein of MW 251,940. Comparison of the HAV nucleotide sequence with that of other picornaviruses has failed to reveal detectable areas of homology. A computer analysis of the putative amino acid sequence of HAV and poliovirus demonstrated the existence of short areas of homology in virion protein 3 and throughout the carboxyl-terminal portion of the polyproteins. In addition, extensive protein structural homologies with poliovirus were detected.Keywords
This publication has 32 references indexed in Scilit:
- Cloning of hepatitis A virus genomeJournal of Virological Methods, 1981
- Primary structure, gene organization and polypeptide expression of poliovirus RNANature, 1981
- Hepatitis A-virus in cell culture: I. Propagation of different hepatitis A-virus isolates in a fetal rhesus monkey kidney cell line (Frhk-4)Medical Microbiology and Immunology, 1980
- Propagation of human hepatitis A virus in a hepatoma cell lineInfection, 1979
- Propagation of Human Hepatitis A Virus in Cell Culture in VitroExperimental Biology and Medicine, 1979
- The Polypeptides of Hepatitis A VirusIntervirology, 1978
- The location of the polio genome protein in viral RNAs and its implication for RNA synthesisNature, 1977
- A protein covalently linked to poliovirus genome RNA.Proceedings of the National Academy of Sciences, 1977
- Prediction of protein conformationBiochemistry, 1974
- Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsBiochemistry, 1974