Abstract
Determination of the complete nucleotide sequence of the avian infectious bronchitis virus IBV genomic RNA (mRNAl), carried out by Boursnell et al. (1987), has shown that the 5′ terminal sequence of mRNA 1 contains two large ORFs, la and lb, which have the potential to encode two polypeptides of molecular weights 441 kDa and 300 kDa, respectively. Several putative functional domains containing well characterised motifs and more complex homologies have been identified in the la or lb regions by computer-aided techniques (Gorbalenya et al., 1989; Lee et al., 1991; Herold et al., 1993). They include proteinase domains and viral RNA replication-related motifs commonly found in positive strand RNA virus genomes (i.e. RNA-dependent-RNA polymerase and RNA helicase motifs). For example, a papain-like and a picornavirus 3C-like proteinase domains were predicted to be located in IBV la (Gorbalenya et al., 1989). However, in mouse hepatitis virus (MHV) and human coronavirus 229E (HCV 229E), two papain-like proteinase domains were found to be located in ORF la region of the genomes (Lee et al., 1991; Herold et al., 1993). The first of these domains in MHV, which is absent in IBV, has been identified to be responsible for proteolytic cleavage of a p28 polypeptide from the la polyprotein (Baker et al., 1989, 1993).
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Baker, S. C, Shieh,C-K., Soe, L. H., Chang, M-F., Vannier, D. M., and Lai, M. M. C. (1989).Identificationof a domain required for autoproteolytic cleavage ofmurine coronavirus gene A polyprotein. J. Virol. 63, 3693–3699.
Baker, S. C.,Yolomori, K., Dong, S., Carlisle, R., Gorbalenya, A. E., Koonin, E. V., andLai, M. M. C. (1993).Identification of the catalytic sites of a papain-likecysteine proteinase of murine coronavirus. J. Virol. 67, 6056–6063.
Blair, W. S., Li,X., and Semler, B. L. (1993). A cellular cofactor facilitates efficient 3CDcleavage of thepoliovirusPl precursor. J. Virol67, 2339–2343.
Boursnell, M. E.G., Brown, T. D. K., Foulds, I. J., Green, P. F., Tomley, F. M., and Binns, M. M. (1987). Completion of the sequence of the genome of the coronavirus avianinfectious bronchitis virus. J. gen. Virol.68, 57–77.
Brierley, I.,Boursnell, M. E. G., Binns, M. M., Bilimoria, B., Rolley, N. J., Brown, T. D.K., and Inglis, S. C.(1990). Products of the polymerase-encoding region ofthe coronavirus IBV. Adv. exp. med. Biol276, 275–278.
Chambers, T. J., Hahn, C. S., Galler, R., and Rice, C.M. (1990). Flavivirus genome organisation, expression, and replication. Annu.Rev. Microbiol.44, 649.
Denison, M. R.,Zoltic, P. W., Hughes, S. A., Giangreco, B., Olson, A. L., Perlman, S.,Leibowitz, J., and Weiss,S. R. (1992). intracellular processing of the N-terminalORF la proteins of the coronavirusMHV-A59requiresmultiples proteolytic events. Virology 189, 274–284.
Dorner, A., Semler, B. L., Jackson, R. J., Hanecak, R., Duprey, E., and Wimmer, E. (1984). In vitrotranslation of poliovirus RNA: Utilisation of internal initiation sites inreticulocyte lysate. J. Virol.50, 507–514.
Dougherty, W. G., and Semler, B. L. (1993). Expression of virus-encodedproteinases: functional and structural similarities with cellular enzymes. MicrobiologicalReviews57, 781–822.
Fuerst, T. R.,Niles, E. G., Studier, F. W., and Moss, B.(1986). Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesises bacteriophage T7 RNApolymerase. Proc. Natl. Acad. Sci. USA83, 8122–8127.
Gorbalenya, A. E.,Koonin, E. V., Donchenko, A. P., and Blinov, V. M. (1989). Coronavirus genome:predictionof putative functional domains in the non-structuralpolyprotein by comparative amino acid sequence analysis. Nucleic AcidsResearch17, 4847–4860.
Herold, J., Raabe, T., Schelle-Prinz,B.,and Siddell, S. G. (1993). Nucleotide sequence of the human coronavirus 229ERNA polymerase locus. Virology195, 680–691.
Lee, H-J., Shieh,C-K., Gorbalenya, A. E., Koonin, E. V., Monica, N. L., Tuler, J.,Bagdzhadzhyan, A., andLai, M. M. C. (1991). The complete sequence (22 kilobases)of murine coronavirus gene 1 encoding the putative proteases and RNApolymerase. Virology180, 567–582.
Liu, D. X.,Brierley, I., Tibbies, K. W., and Brown, T. D. K. (1994). A 100-kilodaltonpolypeptide encoded byopen reading frame (ORF) lb of the coronavirus infectious bronchitis virus is processed by ORF laproducts.J. Virol.68, in press.
Smith, G. L.(1993). Vaccinia virus glycoproteins and immune evasion. J. gen. Virol.74,1725–1740.
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© 1995 Springer Science+Business Media New York
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Liu, D.X., Tibbles, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I. (1995). Involvement of Viral and Cellular Factors in Processing of Polyprotein Encoded by ORF1a of the Coronavirus IBV. In: Talbot, P.J., Levy, G.A. (eds) Corona- and Related Viruses. Advances in Experimental Medicine and Biology, vol 380. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1899-0_67
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