1887

Abstract

Celery latent virus (CeLV) is an incompletely described plant virus known to be sap and seed transmissible and to possess flexuous filamentous particles measuring about 900 nm in length, suggesting it as a possible member of the family Potyviridae. Here, an Italian isolate of CeLV was transmitted by sap to a number of host plants and shown to have a single-stranded and monopartite RNA genome being 11 519 nucleotides (nts) in size and possessing some unusual features. The RNA contains a large open reading frame (ORF) that is flanked by a short 5′ untranslated region (UTR) of 13 nt and a 3′ UTR consisting of 586 nt that is not polyadenylated. CeLV RNA shares nt sequence identity of only about 40 % with other members of the Potyviridae (potyvirids). The CeLV polyprotein is notable in that it starts with a signal peptide, has a putative P3N-PIPO ORF and shares low aa sequence identity (about 18 %) with other potyvirids. Although potential cleavage sites were not identified for the N-terminal two-thirds of the polyprotein, the latter possesses a number of sequence motifs, the identity and position of which are characteristic of other potyvirids. Attempts at constructing an infectious full-length cDNA clone of CeLV were successful following Rhizobium radiobacter infiltration of Nicotiana benthamiana and Apium graveolens. CeLV appears to have the largest genome of all known potyvirids and some unique genome features that may warrant the creation of a new genus, for which we propose the name ‘celavirus’.

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2019-01-22
2019-10-23
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References

  1. Severin HHP, Freitag JH. Western celery mosaic. Hilgardia 1938;11:493–558 [CrossRef]
    [Google Scholar]
  2. Severin HHP. Symptoms of cucumber-mosaic and tobacco-ringspot viruses on celery. Hilgardia 1950;20:267–277 [CrossRef]
    [Google Scholar]
  3. Brandes J, Luisoni E. Untersuchungen über einige Eigenschaften von zwei gestreckten Sellerieviren. J Phytopathol 1966;57:277–288 [CrossRef]
    [Google Scholar]
  4. Bos L, Diaz-Ruiz JR, Maat DZ. Further characterization of celery latent virus. Neth J Plant Pathol 1978;84:61–79 [CrossRef]
    [Google Scholar]
  5. Hollings M, Brunt AA. Potyvirus group. CMI/AAB Descriptions of Plant Viruses 1981;245:
    [Google Scholar]
  6. Wylie SJ, Adams M, Chalam C, Kreuze J, López-Moya JJ et al. Erratum: ICTV Virus Taxonomy Profile: Potyviridae. J Gen Virol 2017;98:2893–354 [CrossRef][PubMed]
    [Google Scholar]
  7. Seo JK, Kwak HR, Kim MK, Kim JS, Choi HS. The complete genome sequence of a novel virus, bellflower veinal mottle virus, suggests the existence of a new genus within the family Potyviridae. Arch Virol 2017;162:2457–2461 [CrossRef][PubMed]
    [Google Scholar]
  8. Mollov D, Lockhart B, Zlesak D. Complete nucleotide sequence of rose yellow mosaic virus, a novel member of the family Potyviridae. Arch Virol 2013;158:1917–1923 [CrossRef][PubMed]
    [Google Scholar]
  9. Davidson AD, Pröls M, Schell J, Steinbiss HH. The nucleotide sequence of RNA 2 of barley yellow mosaic virus. J Gen Virol 1991;72:989–993 [CrossRef][PubMed]
    [Google Scholar]
  10. Kashiwazaki S, Minobe Y, Hibino H. Nucleotide sequence of barley yellow mosaic virus RNA 2. J Gen Virol 1991;72:995–999 [CrossRef][PubMed]
    [Google Scholar]
  11. Kashiwazaki S, Minobe Y, Omura T, Hibino H. Nucleotide sequence of barley yellow mosaic virus RNA 1: a close evolutionary relationship with potyviruses. J Gen Virol 1990;71:2781–2790 [CrossRef][PubMed]
    [Google Scholar]
  12. Urcuqui-Inchima S, Haenni AL, Bernardi F. Potyvirus proteins: a wealth of functions. Virus Res 2001;74:157–175 [CrossRef][PubMed]
    [Google Scholar]
  13. Verchot J, Koonin EV, Carrington JC. The 35-kDa protein from the N-terminus of the potyviral polyprotein functions as a third virus-encoded proteinase. Virology 1991;185:527–535 [CrossRef][PubMed]
    [Google Scholar]
  14. Carrington JC, Cary SM, Parks TD, Dougherty WG. A second proteinase encoded by a plant potyvirus genome. EMBO J 1989;8:365–370 [CrossRef][PubMed]
    [Google Scholar]
  15. Carrington JC, Dougherty WG. Small nuclear inclusion protein encoded by a plant potyvirus genome is a protease. J Virol 1987;61:2540–2548[PubMed]
    [Google Scholar]
  16. Blanc S, López-Moya JJ, Wang R, García-Lampasona S, Thornbury DW et al. A specific interaction between coat protein and helper component correlates with aphid transmission of a potyvirus. Virology 1997;231:141–147 [CrossRef][PubMed]
    [Google Scholar]
  17. Valli AA, Gallo A, Rodamilans B, López-Moya JJ, García JA. The HCPro from the Potyviridae family: an enviable multitasking Helper Component that every virus would like to have. Mol Plant Pathol 2018;19:744–763 [CrossRef][PubMed]
    [Google Scholar]
  18. Olspert A, Chung BY, Atkins JF, Carr JP, Firth AE. Transcriptional slippage in the positive-sense RNA virus family Potyviridae. EMBO Rep 2015;16:995–1004 [CrossRef][PubMed]
    [Google Scholar]
  19. Chung BY, Miller WA, Atkins JF, Firth AE. An overlapping essential gene in the Potyviridae. Proc Natl Acad Sci USA 2008;105:5897–5902 [CrossRef][PubMed]
    [Google Scholar]
  20. Wen RH, Hajimorad MR. Mutational analysis of the putative pipo of soybean mosaic virus suggests disruption of PIPO protein impedes movement. Virology 2010;400:1–7 [CrossRef][PubMed]
    [Google Scholar]
  21. Hillung J, Elena SF, Cuevas JM. Intra-specific variability and biological relevance of P3N-PIPO protein length in potyviruses. BMC Evol Biol 2013;13:249 [CrossRef][PubMed]
    [Google Scholar]
  22. Wei T, Zhang C, Hong J, Xiong R, Kasschau KD et al. Formation of complexes at plasmodesmata for potyvirus intercellular movement is mediated by the viral protein P3N-PIPO. PLoS Pathog 2010;6:e1000962 [CrossRef][PubMed]
    [Google Scholar]
  23. Tatineni S, Qu F, Li R, Morris TJ, French R. Triticum mosaic poacevirus enlists P1 rather than HC-Pro to suppress RNA silencing-mediated host defense. Virology 2012;433:104–115 [CrossRef][PubMed]
    [Google Scholar]
  24. Young BA, Stenger DC, Qu F, Morris TJ, Tatineni S et al. Tritimovirus P1 functions as a suppressor of RNA silencing and an enhancer of disease symptoms. Virus Res 2012;163:672–677 [CrossRef][PubMed]
    [Google Scholar]
  25. Susaimuthu J, Tzanetakis IE, Gergerich RC, Martin RR. A member of a new genus in the Potyviridae infects Rubus. Virus Res 2008;131:145–151 [CrossRef][PubMed]
    [Google Scholar]
  26. Zhang P, Peng J, Guo H, Chen J, Chen S et al. Complete genome sequence of yam chlorotic necrotic mosaic virus from Dioscorea parviflora. Arch Virol 2016;161:1715–1717 [CrossRef][PubMed]
    [Google Scholar]
  27. Minutillo SA, Marais A, Mascia T, Faure C, Svanella-Dumas L et al. Complete Nucleotide Sequence of Artichoke latent virus Shows it to be a Member of the Genus Macluravirus in the Family Potyviridae. Phytopathology 2015;105:1155–1160 [CrossRef][PubMed]
    [Google Scholar]
  28. Kondo T, Fujita T. Complete nucleotide sequence and construction of an infectious clone of Chinese yam necrotic mosaic virus suggest that macluraviruses have the smallest genome among members of the family Potyviridae. Arch Virol 2012;157:2299–2307 [CrossRef][PubMed]
    [Google Scholar]
  29. Abraham A, Menzel W, Vetten HJ, Winter S. Analysis of the tomato mild mottle virus genome indicates that it is the most divergent member of the genus Ipomovirus (family Potyviridae). Arch Virol 2012;157:353–357 [CrossRef][PubMed]
    [Google Scholar]
  30. Colinet D, Kummert J, Lepoivre P. The nucleotide sequence and genome organization of the whitefly transmitted sweetpotato mild mottle virus: a close relationship with members of the family Potyviridae. Virus Res 1998;53:187–196 [CrossRef][PubMed]
    [Google Scholar]
  31. Carbonell A, Dujovny G, García JA, Valli A. The Cucumber vein yellowing virus silencing suppressor P1b can functionally replace HCPro in Plum pox virus infection in a host-specific manner. Mol Plant Microbe Interact 2012;25:151–164 [CrossRef][PubMed]
    [Google Scholar]
  32. Valli A, Dujovny G, García JA. Protease activity, self interaction, and small interfering RNA binding of the silencing suppressor p1b from cucumber vein yellowing ipomovirus. J Virol 2008;82:974–986 [CrossRef][PubMed]
    [Google Scholar]
  33. Valli A, Martín-Hernández AM, López-Moya JJ, García JA. RNA silencing suppression by a second copy of the P1 serine protease of Cucumber vein yellowing ipomovirus, a member of the family Potyviridae that lacks the cysteine protease HCPro. J Virol 2006;80:10055–10063 [CrossRef][PubMed]
    [Google Scholar]
  34. Li W, Hilf ME, Webb SE, Baker CA, Adkins S. Presence of P1b and absence of HC-Pro in Squash vein yellowing virus suggests a general feature of the genus Ipomovirus in the family Potyviridae. Virus Res 2008;135:213–219 [CrossRef][PubMed]
    [Google Scholar]
  35. Janssen D, Martín G, Velasco L, Gómez P, Segundo E et al. Absence of a coding region for the helper component-proteinase in the genome of cucumber vein yellowing virus, a whitefly-transmitted member of the Potyviridae. Arch Virol 2005;150:1439–1447 [CrossRef][PubMed]
    [Google Scholar]
  36. Mbanzibwa DR, Tian Y, Mukasa SB, Valkonen JP. Cassava brown streak virus (Potyviridae) encodes a putative Maf/HAM1 pyrophosphatase implicated in reduction of mutations and a P1 proteinase that suppresses RNA silencing but contains no HC-Pro. J Virol 2009;83:6934–6940 [CrossRef][PubMed]
    [Google Scholar]
  37. Monger WA, Alicai T, Ndunguru J, Kinyua ZM, Potts M et al. The complete genome sequence of the Tanzanian strain of Cassava brown streak virus and comparison with the Ugandan strain sequence. Arch Virol 2010;155:429–433 [CrossRef][PubMed]
    [Google Scholar]
  38. Frohman MA, Dush MK, Martin GR. Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci USA 1988;85:8998–9002 [CrossRef][PubMed]
    [Google Scholar]
  39. Lütcke HA, Chow KC, Mickel FS, Moss KA, Kern HF et al. Selection of AUG initiation codons differs in plants and animals. Embo J 1987;6:43–48 [CrossRef][PubMed]
    [Google Scholar]
  40. Nakagawa S, Niimura Y, Gojobori T, Tanaka H, Miura K. Diversity of preferred nucleotide sequences around the translation initiation codon in eukaryote genomes. Nucleic Acids Res 2008;36:861–871 [CrossRef][PubMed]
    [Google Scholar]
  41. Riechmann JL, Laín S, García JA. Identification of the initiation codon of plum pox potyvirus genomic RNA. Virology 1991;185:544–552 [CrossRef][PubMed]
    [Google Scholar]
  42. Simón-Buela L, Guo HS, García JA. Cap-independent leaky scanning as the mechanism of translation initiation of a plant viral genomic RNA. J Gen Virol 1997;78:2691–2699 [CrossRef][PubMed]
    [Google Scholar]
  43. Letunic I, Doerks T, Bork P. SMART: recent updates, new developments and status in 2015. Nucleic Acids Res 2015;43:D257–D260 [CrossRef][PubMed]
    [Google Scholar]
  44. Schultz J, Milpetz F, Bork P, Ponting CP. SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci USA 1998;95:5857–5864 [CrossRef][PubMed]
    [Google Scholar]
  45. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol 1990;215:403–410 [CrossRef][PubMed]
    [Google Scholar]
  46. Kelley LA, Mezulis S, Yates CM, Wass MN, Sternberg MJ. The Phyre2 web portal for protein modeling, prediction and analysis. Nat Protoc 2015;10:845–858 [CrossRef][PubMed]
    [Google Scholar]
  47. King A. Virus Taxonomy Classification and Nomenclature of viruses; Ninth Report of the International Committee on Taxonomy of Viruses Amsterdam: Elsevier; 2012
    [Google Scholar]
  48. Käll L, Krogh A, Sonnhammer EL. Advantages of combined transmembrane topology and signal peptide prediction–the Phobius web server. Nucleic Acids Res 2007;35:W429–W432 [CrossRef][PubMed]
    [Google Scholar]
  49. Bannai H, Tamada Y, Maruyama O, Nakai K, Miyano S. Extensive feature detection of N-terminal protein sorting signals. Bioinformatics 2002;18:298–305 [CrossRef][PubMed]
    [Google Scholar]
  50. Emanuelsson O, Brunak S, von Heijne G, Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2007;2:953–971 [CrossRef][PubMed]
    [Google Scholar]
  51. Adams MJ, Antoniw JF, Fauquet CM. Molecular criteria for genus and species discrimination within the family Potyviridae. Arch Virol 2005;150:459–479 [CrossRef][PubMed]
    [Google Scholar]
  52. Pasin F, Simón-Mateo C, García JA. The hypervariable amino-terminus of P1 protease modulates potyviral replication and host defense responses. PLoS Pathog 2014;10:e1003985 [CrossRef][PubMed]
    [Google Scholar]
  53. Valli A, López-Moya JJ, García JA. Recombination and gene duplication in the evolutionary diversification of P1 proteins in the family Potyviridae. J Gen Virol 2007;88:1016–1028 [CrossRef][PubMed]
    [Google Scholar]
  54. Rohozková J, Šebela M, Navrátil M. P1 peptidase of Pea seed-borne mosaic virus contains non-canonical C2H2 zinc finger and may act in a truncated form. J Plant Sci Mol Breed 2014;3:1 [CrossRef]
    [Google Scholar]
  55. Rohozková J, Navrátil M. P1 peptidase–a mysterious protein of family Potyviridae. J Biosci 2011;36:189–200 [CrossRef][PubMed]
    [Google Scholar]
  56. Adams MJ, Antoniw JF, Beaudoin F. Overview and analysis of the polyprotein cleavage sites in the family Potyviridae. Mol Plant Pathol 2005;6:471–487 [CrossRef][PubMed]
    [Google Scholar]
  57. Martínez F, Daròs JA. Tobacco etch virus protein P1 traffics to the nucleolus and associates with the host 60S ribosomal subunits during infection. J Virol 2014;88:10725–10737 [CrossRef][PubMed]
    [Google Scholar]
  58. Atreya CD, Pirone TP. Mutational analysis of the helper component-proteinase gene of a potyvirus: effects of amino acid substitutions, deletions, and gene replacement on virulence and aphid transmissibility. Proc Natl Acad Sci USA 1993;90:11919–11923 [CrossRef][PubMed]
    [Google Scholar]
  59. Cronin S, Verchot J, Haldeman-Cahill R, Schaad MC, Carrington JC. Long-distance movement factor: a transport function of the potyvirus helper component proteinase. Plant Cell 1995;7:549–559 [CrossRef][PubMed]
    [Google Scholar]
  60. Gal-On A. A point mutation in the FRNK motif of the potyvirus helper component-protease gene alters symptom expression in cucurbits and elicits protection against the severe homologous virus. Phytopathology 2000;90:467–473 [CrossRef][PubMed]
    [Google Scholar]
  61. Granier F, Durand-Tardif M, Casse-Delbart F, Lecoq H, Robaglia C. Mutations in zucchini yellow mosaic virus helper component protein associated with loss of aphid transmissibility. J Gen Virol 1993;74:2737–2742 [CrossRef][PubMed]
    [Google Scholar]
  62. Huet H, Gal-On A, Meir E, Lecoq H, Raccah B. Mutations in the helper component protease gene of zucchini yellow mosaic virus affect its ability to mediate aphid transmissibility. J Gen Virol 1994;75:1407–1414 [CrossRef][PubMed]
    [Google Scholar]
  63. Oh CS, Carrington JC. Identification of essential residues in potyvirus proteinase HC-Pro by site-directed mutagenesis. Virology 1989;173:692–699[PubMed]
    [Google Scholar]
  64. Shiboleth YM, Haronsky E, Leibman D, Arazi T, Wassenegger M et al. The conserved FRNK box in HC-Pro, a plant viral suppressor of gene silencing, is required for small RNA binding and mediates symptom development. J Virol 2007;81:13135–13148 [CrossRef][PubMed]
    [Google Scholar]
  65. Mangrauthia SK, Jain RK, Praveen S. Sequence motifs comparisons establish a functional portrait of a multifunctional protein hc-pro from papaya ringspot potyvirus. J Plant Biochem Biotechnol 2008;17:201–204 [CrossRef]
    [Google Scholar]
  66. Varrelmann M, Maiss E, Pilot R, Palkovics L. Use of pentapeptide-insertion scanning mutagenesis for functional mapping of the plum pox virus helper component proteinase suppressor of gene silencing. J Gen Virol 2007;88:1005–1015 [CrossRef][PubMed]
    [Google Scholar]
  67. Laín S, Riechmann JL, Martín MT, García JA. Homologous potyvirus and flavivirus proteins belonging to a superfamily of helicase-like proteins. Gene 1989;82:357–362 [CrossRef][PubMed]
    [Google Scholar]
  68. Sorel M, Garcia JA, German-Retana S. The Potyviridae cylindrical inclusion helicase: a key multipartner and multifunctional protein. Mol Plant Microbe Interact 2014;27:215–226 [CrossRef][PubMed]
    [Google Scholar]
  69. Kadaré G, Haenni AL. Virus-encoded RNA helicases. J Virol 1997;71:2583–2590[PubMed]
    [Google Scholar]
  70. Koonin EV. The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses. J Gen Virol 1991;72:2197–2206 [CrossRef][PubMed]
    [Google Scholar]
  71. Domier LL, Shaw JG, Rhoads RE. Potyviral proteins share amino acid sequence homology with picorna-, como-, and caulimoviral proteins. Virology 1987;158:20–27 [CrossRef][PubMed]
    [Google Scholar]
  72. Sankaralingam A, Baranwal VK, Ahlawat YS, Devi R, Ramiah M. RT-PCR detection and molecular characterization of Banana bract mosaic virus from the pseudostem and bract of banana. Archives of Phytopathology and Plant Protection 2006;39:273–281 [CrossRef]
    [Google Scholar]
  73. Sudheera Y, Vishnu Vardhan GP, Hema M, Krishna Reddy M, Sreenivasulu P. Characterization of a potyvirus associated with yellow mosaic disease of jasmine (Jasminum sambac L.) in Andhra Pradesh, India. Virusdisease 2014;25:394–397 [CrossRef][PubMed]
    [Google Scholar]
  74. Atreya CD, Raccah B, Pirone TP. A point mutation in the coat protein abolishes aphid transmissibility of a potyvirus. Virology 1990;178:161–165 [CrossRef][PubMed]
    [Google Scholar]
  75. Atreya PL, Lopez-Moya JJ, Chu M, Atreya CD, Pirone TP. Mutational analysis of the coat protein N-terminal amino acids involved in potyvirus transmission by aphids. J Gen Virol 1995;76:265–270 [CrossRef][PubMed]
    [Google Scholar]
  76. Kormelink R, de Haan P, Meurs C, Peters D, Goldbach R. The nucleotide sequence of the M RNA segment of tomato spotted wilt virus, a bunyavirus with two ambisense RNA segments. J Gen Virol 1992;73:2795–2804 [CrossRef][PubMed]
    [Google Scholar]
  77. de Oliveira AS, Melo FL, Inoue-Nagata AK, Nagata T, Kitajima EW et al. Characterization of bean necrotic mosaic virus: a member of a novel evolutionary lineage within the Genus Tospovirus. PLoS One 2012;7:e38634 [CrossRef][PubMed]
    [Google Scholar]
  78. Ribeiro D, Foresti O, Denecke J, Wellink J, Goldbach R et al. Tomato spotted wilt virus glycoproteins induce the formation of endoplasmic reticulum- and Golgi-derived pleomorphic membrane structures in plant cells. J Gen Virol 2008;89:1811–1818 [CrossRef][PubMed]
    [Google Scholar]
  79. Chen T-C, Li J-T, Lin Y-P, Yeh Y-C, Kang Y-C et al. Genomic characterization of Calla lily chlorotic spot virus and design of broad-spectrum primers for detection of tospoviruses. Plant Pathol 2012;61:183–194 [CrossRef]
    [Google Scholar]
  80. Schaad MC, Jensen PE, Carrington JC. Formation of plant RNA virus replication complexes on membranes: role of an endoplasmic reticulum-targeted viral protein. EMBO J 1997;16:4049–4059 [CrossRef][PubMed]
    [Google Scholar]
  81. Wei T, Huang TS, McNeil J, Laliberté JF, Hong J et al. Sequential recruitment of the endoplasmic reticulum and chloroplasts for plant potyvirus replication. J Virol 2010;84:799–809 [CrossRef][PubMed]
    [Google Scholar]
  82. Menzel W, Jelkmann W, Maiss E. Detection of four apple viruses by multiplex RT-PCR assays with coamplification of plant mRNA as internal control. J Virol Methods 2002;99:81–92 [CrossRef][PubMed]
    [Google Scholar]
  83. Morris TJ. Isolation and analysis of double-stranded RNA from virus-infected plant and fungal tissue. Phytopathology 1979;69:854 [CrossRef]
    [Google Scholar]
  84. Froussard P. A random-PCR method (rPCR) to construct whole cDNA library from low amounts of RNA. Nucleic Acids Res 1992;20:2900 [CrossRef][PubMed]
    [Google Scholar]
  85. Kumar S, Stecher G, Tamura K. MEGA7: molecular evolutionary genetics analysis version 7.0 for Bigger Datasets. Mol Biol Evol 2016;33:1870–1874 [CrossRef][PubMed]
    [Google Scholar]
  86. Edgar RC. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 2004;32:1792–1797 [CrossRef][PubMed]
    [Google Scholar]
  87. Nei M, Kumar S. Molecular Evolution and Phylogenetics 2000
    [Google Scholar]
  88. Gibson DG, Young L, Chuang RY, Venter JC, Hutchison CA et al. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat Methods 2009;6:343–345 [CrossRef][PubMed]
    [Google Scholar]
  89. Xiang C, Han P, Lutziger I, Wang K, Oliver DJ. A mini binary vector series for plant transformation. Plant Mol Biol 1999;40:711–717 [CrossRef][PubMed]
    [Google Scholar]
  90. Hanahan D. Studies on transformation of Escherichia coli with plasmids. J Mol Biol 1983;166:557–580 [CrossRef]
    [Google Scholar]
  91. Birnboim HC, Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res 1979;7:1513–1523 [CrossRef][PubMed]
    [Google Scholar]
  92. Hellens R, Mullineaux P, Klee H, Focus T. A guide to Agrobacterium binary Ti vectors. Trends in Plant Science 2000;5:446–451
    [Google Scholar]
  93. Mattanovich D, Rüker F, Machado AC, Laimer M, Regner F et al. Efficient transformation of Agrobacterium spp. by electroporation. Nucleic Acids Res 1989;17:6747 [CrossRef][PubMed]
    [Google Scholar]
  94. Lesemann DE. EM-characterization of virus particles and non-structural viral proteins in plant extracts and in infected cells. In Lapierre H, Signoret PA. (editors) Viruses and Virus Diseases of Poaceae (Gramineae) Paris, Enfield, N.H: INRA; 2004; pp.92–94
    [Google Scholar]
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