Summary
Currently available sequence information suggests that the genome organization of hepatitis C virus is similar to that of flaviviruses. A positive-stranded genomic RNA contains a single long open reading frame (ORF) which is flanked by 5′ and 3′ noncoding sequences. This RNA codes for structural proteins at the 5′ end (starting with the capsid protein) and a set of nonstructural proteins in the remainder of the genome. The latter provide essential virus-specific functions for the viral life cycle, such as protease, helicase, and RNA replicase activities. The sequence motifs characteristic of the corresponding functional protein domains are separated by similar spacings in the nonstructural regions of hepatitis C virus and flaviviruses. The structural region of the hepatitis C virus appears to consist of a capsid protein which is larger than that of flaviviruses and two putative envelope proteins which are presumably different in molecular weight and much more heavily glycosylated than their counterparts in flaviviruses. A study group of the International Committee on the Taxonomy of viruses proposes to include hepatitis C virus as a genus into the family ‘flaviviridae’.
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References
Bazan JF, Fletterick RJ (1989) Detection of a trypsin like serine protease domain in flaviviruses and pestiviruses. Virology 171: 637–639
Chambers TJ, Hahn CS, Galler R, Rice CM (1990) Flavivirus genome organization, expression and replication. Ann Rev Microbiol 44: 649–688
Choo QL, Kuo G, Weiner AJ, Överby LR, Bradley DW, Houghton M (1989) Isolation of a cDNA clone derived from a blood-borne non-A, non-B hepatitis genome. Science 244: 359–362
Flanegan JB, Baltimore D (1977) Polio virus-specific primer-dependent RNA poly¬merase able to copy poly(A). Proc Natl Acad Sci USA 74: 2677–2680
Gibbs A (1987) Molecular evolution of viruses: ‘trees’, ‘clocks’ and ‘modules’. J Cell Sci 7: 319–337
Goldbach R (1990) Genome similarities between positive-strand viruses from plants and animals. In: Brinton MA, Heinz FX (eds) New aspects of positive-strand RNA viruses. American Society for Microbiology, Washington, DC, pp 3–11
Gorbalanya AE, Koonin EV, Donchenko AP, Blinov VM (1988) A novel superfamily of nucleoside triphosphate binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination. FEBS Lett 235: 16–24
Gorbalanya AE, Donchenko AP, Koonin EV, Blinov VM (1989) N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases. Nucleic Acids Res 17: 3889–3897
Hodgman TC (1988) A new superfamily of replicative proteins. Nature 333: 22–23
Houghton M, Choo QL, Kuo G (1988) NANBV diagnostics and vaccines. Europ Pat Appl Nr 88310922.5; Publ No. 318216
Kamer G, Arges P (1989) Primary structural comparison of RNA-dependent polymerases from plant, animal and bacterial viruses. Nucleic Acids Res 12: 7269–7282
Lain S, Riechmann JL, Martin MT, Garcia JA (1989) Homologous potyvirus and flavivirus proteins belonging to a superfamily of helicase-like proteins. Gene 82: 357–362
Lundquist RE, Ehrenfeld E, Maizel JV (1974) Isolation of a viral polypeptide associated with poliovirus RNA polymerase. Proc Natl Acad Sei USA 71: 4773–4777
Mandl CW, Heinz FX, Kunz C (1991) Presence of poly(A) in a flavivirus: Significant differences between the 3′ noncoding regions of the genomic RNAs of Tick-borne encephalitis virus strains.
Miller RH, Purcell RH (1990) Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus supergroups. Proc Natl Acad Sci USA 87: 2057–2061
Monath T (1990) Flaviviruses. In: Fields BN, Knipe DM (eds) Virology, 2nd edn. Raven Press, New York, pp 763–814
Okamoto H, Okada S, Sugiyama Y, Yotsumoto S, Tanaka T, Yoshizawa H, Tsuda F, Miyokawa Y, Mayumi M (1990) The 5’-terminal sequence of the hepatitis C virus genome. Japan J Exp Med 60: 167–177
Preugschat F, Yao C-W, Strauss JH (1990) In vitro processing of dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3. J Virol 64: 4364–4374
Randolph VB, Winkler B, Stollar V (1990) Acidotropic amines inhibit proteolytic processing of flavivirus prM protein. Virology 174: 450–458
Shapiro D, Brandt W, Russell PK (1972) Change involving a viral membrane glycoprotein during morphogenesis of group B Arboviruses. Virology 50: 906–911
Takeuchi K, Kubo Y, Boonmar S, Watanabe Y, Katayama T, Choo QL, Kuo G, Houghton M, Saito I, Miyamura T (1991). The putative nucleocapsid and envelope protein genes of hepatitis C virus determined by comparison of the nucleotide sequences of two isolates derived from an experimentally infected chimpanzee and healthy human carriers. J Gen Virol 71: 3027–3033
Von Heijne G (1984) How signal sequences maintain cleavage specificity. J Mol Biol 173:243–251
Wengler G, Castle E, Leidner U, Nowak T, Wengler G (1985) Sequence analysis of the membrane protein V3 of the flavivirus West Nile virus and of its gene. Virology 147: 264–274
Zimmern D (1987) Evolution of RNA viruses. In: Holland J, Domingo E, Ahlquist P (eds) RNA genetics. CRC Press, Boca Raton, FL, pp 211–240
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© 1992 Springer-Verlag
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Heinz, F.X. (1992). Comparative molecular biology of flaviviruses and hepatitis C virus. In: De Bac, C., Taliani, G., Gerlich, W.H. (eds) Chronically Evolving Viral Hepatitis. Archives of Virology, vol 4. Springer, Vienna. https://doi.org/10.1007/978-3-7091-5633-9_35
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DOI: https://doi.org/10.1007/978-3-7091-5633-9_35
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