Biopolym. Cell. 2003; 19(2):140-150.
Structure and Function of Biopolymers
Comparative analysis of primary and secondary structures of carlaviruses' capsid proteins
- Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine
1, Murmans'ka Str., Kyiv, Ukraine, 02094
Abstract
The primary and secondary structures of 23 carlaviruses' capsid proteins have been analysed. As a result of the primary structure analysis by multiple alignment seven motifs have been established, three of them being specific for the carlaviruses' capsid proteins. The secondary structure analysis by means of multiple comparison has shown a high degree of secondary structure conservatism in the core and C-terminal regions, and considerable variability in the N-terminus. A general scheme for the secondary structure of the carlaviruses' capsid proteins has been proposed, on the base of multiple comparison results.
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References
[1]
Wetter C, Milne RG. Carlaviruses. Handbook of plant virus infections and comparative diagnosis. Ed. E. Kurstak. Amsterdam: Elsevier, 1981: 695-730.
[2]
Zavriev SK, Kanyuka KV, Levay KE. The genome organization of potato virus M RNA. J Gen Virol. 1991;72 (Pt 1):9-14.
[3]
Cavileer TD, Halpern BT, Lawrence DM, Podleckis EV, Martin RR, Hillman BI. Nucleotide sequence of the carlavirus associated with blueberry scorch and similar diseases. J Gen Virol. 1994;75 ( Pt 4):711-20.
[4]
Hataya T, Uchino K, Arimoto R, Suda N, Sano T, Shikata E, Uyeda I. Molecular characterization of Hop latent virus and phylogenetic relationships among viruses closely related to carlaviruses. Arch Virol. 2000;145(12):2503-24.
[5]
Fuji S, Yamamoto H, Inoue M, Yamashita K, Fukui Y, Furuya H, Naito H. Complete nucleotide sequence of the genomic RNA of Aconitum latent virus (genus Carlavirus) isolated from Delphinium sp.. Arch Virol. 2002;147(4):865-70.
[6]
Chen J, Chen J, Adams MJ. Molecular characterisation of a complex mixture of viruses in garlic with mosaic symptoms in China. Arch Virol. 2001;146(10):1841-53.
[7]
Foster GD. The structure and expression of the genome of carlaviruses. Res Virol. 1992;143(2):103-12.
[8]
Bhyravbhatla B, Watowich SJ, Caspar DL. Refined atomic model of the four-layer aggregate of the tobacco mosaic virus coat protein at 2.4-A resolution. Biophys J. 1998;74(1):604-15.
[9]
Wang H, Planchart A, Allen D, Pattanayek R, Stubbs G. Preliminary X-ray diffraction studies of ribgrass mosaic virus. J Mol Biol. 1993;234(3):902-4.
[10]
Wang H, Stubbs G. Structure determination of cucumber green mottle mosaic virus by X-ray fiber diffraction. Significance for the evolution of tobamoviruses. J Mol Biol. 1994;239(3):371-84.
[11]
Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994;22(22):4673-80.
[12]
Gattiker A, Gasteiger E, Bairoch A. ScanProsite: a reference implementation of a PROSITE scanning tool. Appl Bioinformatics. 2002;1(2):107-8.
[13]
Geourjon C, Del?age G. SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput Appl Biosci. 1995;11(6):681-4.
[14]
Gramstat A, Courtpozanis A, Rohde W. The 12 kDa protein of potato virus M displays properties of a nucleic acid-binding regulatory protein. FEBS Lett. 1990;276(1-2):34-8.
[15]
Foster GD, Mills PR. The 3'-nucleotide sequence of an ordinary strain of potato virus S. Virus Genes. 1992;6(3):213-20.
[16]
MacKenzie DJ, Tremaine JH, Stace-Smith R. Organization and interviral homologies of the 3'-terminal portion of potato virus S RNA. J Gen Virol. 1989;70 ( Pt 5):1053-63.
[17]
Foster GD, Millar AW, Meehan BM, Mills PR. Nucleotide sequence of the 3'-terminal region of Helenium virus S RNA. J Gen Virol. 1990;71 ( Pt 8):1877-80.
[18]
Memelink J, van der Vlugt CI, Linthorst HJ, Derks AF, Asjes CJ, Bol JF. Homologies between the genomes of a carlavirus (lily symptomless virus) and a potexvirus (lily virus X) from lily plants. J Gen Virol. 1990;71 ( Pt 4):917-24.
[19]
Ahn HI, Ryu JH, Kim JK, Lee SY, Choi JK, Park WM, Ryu KH. Nucleotide sequence analysis of the 3'-terminal region of two Korean isolates of lily symptomless Carlavirus and expression of the coat protein in E. coli. Mol Cells. 1999;9(3):338-43.
[20]
Meehan BM, Mills PR. Nucleotide sequence of the 3'-terminal region of carnation latent virus. Intervirology. 1991;32(4):262-7.
[21]
Henderson J, Gibbs MJ, Edwards ML, Clarke VA, Gardner KA, Cooper JI. Partial nucleotide sequence of poplar mosaic virus RNA confirms its classification as a carlavirus. J Gen Virol. 1992;73 ( Pt 7):1887-90.
[22]
Hataya T, Arimoto R, Suda N, Uyeda I. Molecular characterization of Hop mosaic virus: its serological and molecular relationships to Hop latent virus. Arch Virol. 2001;146(10):1935-48.
[23]
Nicolaisen M, Nielsen SL. Analysis of the triple gene block and coat protein sequences of two strains of Kalancho? latent carlavirus. Virus Genes. 2001;22(3):265-70.
[24]
Tsuneyoshi T, Matsumi T, Deng TC, Sako I, Sumi S. Differentiation of Allium carlaviruses isolated from different parts of the world based on the viral coat protein sequence. Arch Virol. 1998;143(6):1093-107.
[25]
Levay K, Zavriev S. Nucleotide sequence and gene organization of the 3'-terminal region of chrysanthemum virus B genomic RNA. J Gen Virol. 1991;72 ( Pt 10):2333-7.
[26]
Ryu JH, Park HW, Park WM, Lee SY, Ryu KH. Molecular analysis of the 3'-terminal region of lily latent Carlavirus from Lilium lancitoium. Plant Pathol. 2000; 16(4): 231-5.
[27]
Naidu RA, Gowda S, Satyanarayana T, Boyko V, Reddy AS, Dawson WO, Reddy DV. Evidence that whitefly-transmitted cowpea mild mottle virus belongs to the genus Carlavirus. Arch Virol. 1998;143(4):769-80.
[28]
Combet C, Blanchet C, Geourjon C, Del?age G. NPS@: network protein sequence analysis. Trends Biochem Sci. 2000;25(3):147-50.
[29]
Adams AN, Barbara DJ. The use of F(ab‘) 2 -based ELISA to detect serological relationships among carlaviruses . Ann Applied Biology. 1982;101(3):495–500.
[30]
Hewish DR, Xiao XW, Mishra A, Gough KH, Shukla DD. Characterisation and epitope analysis of monoclonal antibodies to virions of clover yellow vein and Johnsongrass mosaic potyviruses. Arch Virol. 1993;133(1-2):127-41.
[31]
Shukla DD, Strike PM, Tracy SL, Gough KH, Ward CW. The N and C Termini of the Coat Proteins of Potyviruses Are Surface-located and the N Terminus Contains the Major Virus-specific Epitopes. J Gen Virol. 1988;69(7):1497–508.
[32]
Commandeur U, Koenig R, Lesemann DE, Torrance L, Burgermeister W, Liu Y, Schots A, Alric M, Grassi G. Epitope mapping on fragments of beet necrotic yellow vein virus coat protein. J Gen Virol. 1992;73 ( Pt 3):695-700.
[33]
Radavsky YuL, Viter SS, Turova IP, Zaitseva LS, J?rvek?lg LV, Saarma MJu, Grebenshchikov NI, Baratova LA. Antigenic structure of the potato virus X coat protein. II. Localization of antigenic determinant(s) at the N-terminus of the protein. Bioorg Khim. 1989, 15 (5):615-9
[34]
Cerovsk? N, Filigarov? M, Subr Z. Partial antigenic characterization of potato virus S (Andean strain) by monoclonal antibodies. Acta Virol. 1996;40(1):23-6.
[35]
Viter SS, Tkachenko TYu, Kolomietz LP, Radavsky YuL. Analysis of antigenic structure of Potato Virus M Ukrainian strains. Biopolym Cell. 2000;16(4):312-19.
[36]
Bloomer AC, Champness JN, Bricogne G, Staden R, Klug A. Protein disk of tobacco mosaic virus at 2.8 A resolution showing the interactions within and between subunits. Nature. 1978;276(5686):362-8.
[37]
Baratova LA, Grebenshchikov NI, Shishkov AV, Kashirin IA, Radavsky JL, J?rvek?lg L, Saarma M. The topography of the surface of potato virus X: tritium planigraphy and immunological analysis. J Gen Virol. 1992;73 ( Pt 2):229-35.
[38]
Dolja VV, Boyko VP, Agranovsky AA, Koonin EV. Phylogeny of capsid proteins of rod-shaped and filamentous RNA plant viruses: two families with distinct patterns of sequence and probably structure conservation. Virology. 1991;184(1):79-86.
[39]
Abouhaidar MG, Lai R. Nucleotide sequence of the 3'-terminal region of clover yellow mosaic virus RNA. J Gen Virol. 1989;70 ( Pt 7):1871-5.
[40]
Foster GD, Mills PR. Translation of potato virus S RNA in vitro: evidence of protein processing. Virus Genes. 1992;6(1):47-52.
[41]
Lawrence DM, Rozanov MN, Hillman BI. Autocatalytic processing of the 223-kDa protein of blueberry scorch carlavirus by a papain-like proteinase. Virology. 1995;207(1):127-35.
[42]
Pereira LG, Torrance L, Roberts IM, Harrison BD. Antigenic structure of the coat protein of potato mop-top furovirus. Virology. 1994;203(2):277-85.