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Chapter 17 : Coding Biases and Viral Fitness

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Abstract:

Codon usage bias has also been described for DNA and RNA viruses. Among the latter, poliovirus (PV) has selected through a codon bias similar to that of its human host species (“optimized”), while the codon bias of hepatitis A virus (HAV) is very different from that of its host (“deoptimized”). Picornavirus internal ribosome entry site (IRES) types have probably evolved by gradual addition of domains and elements that improved their function in ribosome recruitment or otherwise conferred regulation to the process of viral protein synthesis in a specific cell environment. The highly inefficient IRES combined with the lack of a mechanism to induce cellular shutoff leads in HAV to an unfair competition for the cellular translational machinery. An intriguing connection exists between codon bias, codon pair bias, and dinucleotide bias in mammalian genomes. Viral genomes, especially of RNA viruses and retroviruses, are short enough to make them amenable to whole-genome synthesis with currently available technology. Such freedom of design can provide tremendous power to reengineer DNA- and RNA-coding sequences at will to study the impact on viral fitness of large-scale changes in codon bias, codon pair bias, dinucleotide biases, GC content, RNA secondary structures, and other sequence signatures, with the aim to develop a new platform for vaccine design and genetic engineering. The codon usage selected through evolution by PV, HAV and its contribution to their in vivo fitness are still not completely elucidated, but it is certainly remarkable how they follow clearly different strategies.

Citation: Bosch A, Mueller S, Pintó R. 2010. Coding Biases and Viral Fitness, p 271-283. In Ehrenfeld E, Domingo E, Roos R (ed), The Picornaviruses. ASM Press, Washington, DC. doi: 10.1128/9781555816698.ch17
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Figures

Image of Figure 1.
Figure 1.

Fitness loss of HAV and fitness gain of PV as a response to ActD-induced cellular shutoff. Viruses produced in the presence of 0.05 and 0.2 μg of ActD/ml in comparison with virus produced in the absence of the drug are depicted. The mean titer of 11 virus passages in the absence of the drug was given an arbitrary value of 100. The mean titer of 11 passages of the viruses propagated in the presence of ActD is expressed as the percentage of production in the absence of the drug.

Citation: Bosch A, Mueller S, Pintó R. 2010. Coding Biases and Viral Fitness, p 271-283. In Ehrenfeld E, Domingo E, Roos R (ed), The Picornaviruses. ASM Press, Washington, DC. doi: 10.1128/9781555816698.ch17
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Image of Figure 2.
Figure 2.

Fitness loss followed by fitness recovery during the processes of HAV adaptation to different ActD concentrations. Infectious HAV titer production per cell is shown during the first 20 adaptation passages from 0.00 to 0.05, from 0.05 to 0.0, from 0.05 to 0.2, and from 0.2 to 0.05 μg of ActD/ml. TCID, 50% tissue culture infective dose.

Citation: Bosch A, Mueller S, Pintó R. 2010. Coding Biases and Viral Fitness, p 271-283. In Ehrenfeld E, Domingo E, Roos R (ed), The Picornaviruses. ASM Press, Washington, DC. doi: 10.1128/9781555816698.ch17
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Image of Figure 3.
Figure 3.

Growth competition experiments showing the strong virus adaptation to the host microenvironment induced by ActD (abbreviated as AMD in the figure). (Top) Populations adapted to growth in the absence and in the presence of 0.05 μg of ActD/ml were mixed at a 1:1 ratio and grown in the presence of 0.05 μg of ActD/ml. (Bottom) Populations adapted to growth with 0.05 and 0.2 μg of ActD/ml were mixed at a 1:1 ratio and grown in the presence of 0.2 μg of ActD/ml.

Citation: Bosch A, Mueller S, Pintó R. 2010. Coding Biases and Viral Fitness, p 271-283. In Ehrenfeld E, Domingo E, Roos R (ed), The Picornaviruses. ASM Press, Washington, DC. doi: 10.1128/9781555816698.ch17
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Image of Figure 4.
Figure 4.

A genomic analysis of populations adapted to replication in the presence of ActD shows its association with a change in codon usage in the structural protein-coding region but not in the polymerase region. The relative proportion (percentage) of the newly generated codons detected during the process of HAV adaptation to ActD is shown. Codons are sorted as being similarly frequent (black), less frequent (light gray), or more frequent (dark gray) than the original ones with respect to cell host codon usage. (A) Codon usage variation in the capsid region in the absence of ActD. (B) Codon usage variation in the capsid region in the presence of 0.05 μg of ActD/ml from passages 4 to 85 and in the presence of 0.2 μg of ActD/ml from passages 20 (20′) to 38 (38′). (C) Codon usage variation in the polymerase region in the absence of ActD. (D) Codon usage variation in the polymerase region in the presence of 0.05 μg of ActD from passages 4 to 85 and in the presence of 0.2 μg of ActD/ml from passages 20 (20′) to 38 (38′).

Citation: Bosch A, Mueller S, Pintó R. 2010. Coding Biases and Viral Fitness, p 271-283. In Ehrenfeld E, Domingo E, Roos R (ed), The Picornaviruses. ASM Press, Washington, DC. doi: 10.1128/9781555816698.ch17
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Image of Figure 5.
Figure 5.

Capsid folding is independent of Hsp90 in HAV and dependent on Hsp90 in PV. Relative infectious rates for HAV and PV per cell in the presence of increasing concentrations of geldanamycin, an Hsp90 inhibitor ( ), are shown. Viral production at each geldanamycin concentration is expressed as a percentage of viral production in the absence of the drug. IC, 50% inhibitory concentration.

Citation: Bosch A, Mueller S, Pintó R. 2010. Coding Biases and Viral Fitness, p 271-283. In Ehrenfeld E, Domingo E, Roos R (ed), The Picornaviruses. ASM Press, Washington, DC. doi: 10.1128/9781555816698.ch17
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Image of Figure 6.
Figure 6.

(A) Calculated CPB scores for all 14,795 annotated human genes. Each dot represents the calculated CPB score of a gene plotted against its amino acid length. Underrepresented codon pairs yield negative scores. Various PV constructs are represented by symbols: PV(M)-wt, wt PV (CPB = –0.02). Lower CPB scores result in lower translation and higher attenuation. (B) Structures of the various chimeric, partly synthetic PV constructs and their viabilities in cultured cells. Nucleotide positions in the viral genome are shown. (C) One-step growth curve with respect to PFU. A multiplicity of infection of 2 was used to infect a monolayer of HeLa R19 cells. Symbols: open squares, PV(M)-wt; solid circles, PV-Max; open diamonds, PV-Min755-1513; asterisks, PV-Min1513-2470; solid diamonds, PV-MinXY; open triangles, PV-MinZ. (D) Same experiment as in panel C, but with results graphed with respect to the number of viral particles instead of PFU. (E) Plaque phenotypes of viruses after 72 h of incubation and staining with crystal violet (plate diameter, 35 mm). (Modified from Coleman et al., 2008 [ ].)

Citation: Bosch A, Mueller S, Pintó R. 2010. Coding Biases and Viral Fitness, p 271-283. In Ehrenfeld E, Domingo E, Roos R (ed), The Picornaviruses. ASM Press, Washington, DC. doi: 10.1128/9781555816698.ch17
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Image of Figure 7.
Figure 7.

In PV, translational selection, i.e., the adaptation of codon usage to cellular codon usage and thus to the tRNA pools for a quantitatively highly efficient and accurate rate of translation, is the main driving evolutionary force of codon usage. The avoidance of certain codon pair combinations (codon pair bias) that slow down the translational rate is an additional regulation step for highly efficient translation. In contrast, in HAV, fine-tuning translation kinetics selection, i.e., the right combination of common and rare codons allowing a regulated ribosome traffic rate to ensure proper protein folding, is the main driving evolutionary force of its codon usage. Ribosome stallings at rare codon positions allow a sequential folding. When such a combination is lost due to a change in the tRNA pools (i.e., artificial shutoff induced by ActD [abbreviated as AMD in the figure]), capsid folding is altered and a readaptation of codon usage takes place to regain the kinetics of translation and proper protein folding.

Citation: Bosch A, Mueller S, Pintó R. 2010. Coding Biases and Viral Fitness, p 271-283. In Ehrenfeld E, Domingo E, Roos R (ed), The Picornaviruses. ASM Press, Washington, DC. doi: 10.1128/9781555816698.ch17
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References

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1. Abad, F. X.,, R. M. Pinto, and, A. Bosch. 1994. Survival of enteric viruses on environmental fomites. Appl. Environ. Microbiol. 60:37043710.
2. Abad, F. X.,, R. M. Pinto,, J. M. Diez, and, A. Bosch. 1994. Disinfection of human enteric viruses in water by copper and silver in combination with low levels of chlorine. Appl. Environ. Microbiol. 60:23772383.
3. Aragones, L.,, A. Bosch, and, R. M. Pintó. 2008. Hepatitis A virus mutant spectra under the selective pressure of monoclonal antibodies: codon usage constraints limit capsid variability. J. Virol. 82:16881700.
4. Aragones, L.,, S. Guix,, E. Ribes,, A. Bosch, and, R. M. Pinto. 2010. Fine-tuning translation kinetics selection as the driving force of codon usage bias in the hepatitis A virus capsid. PLoS Pathog. 6:e1000797.
5. Bennetzen, J. L., and, B. D. Hall. 1982. Codon selection in yeast. J. Biol. Chem. 257:30263031.
6. Bishop, N. E.,, D. L. Hugo,, S. V. Borovec, and, D. A. Anderson. 1994. Rapid and efficient purification of hepatitis A virus from cell culture. J. Virol. Methods 47:203216.
7. Borman, A. M.,, R. Kirchweger,, E. Ziegler,, R. E. Rhoads,, T. Skern, and, K. M. Kean. 1997. elF4G and its proteolytic cleavage products: effect on initiation of protein synthesis from capped, uncapped, and IRES-containing mRNAs. RNA 3:186196.
8. Bosch, A.,, F. Lucena,, J. M. Diez,, R. Gajardo, and, M. Blasi. 1991. Waterborne viruses associated with hepatitis outbreak. J. Am. Water Works Assoc. 83:8083.
9. Brown, E. A.,, A. J. Zajac, and, S. M. Lemon. 1994. In vitro characterization of an internal ribosomal entry site (IRES) present within the 5′ nontranslated region of hepatitis A virus RNA: comparison with the IRES of encephalomyocarditis virus. J. Virol. 68:10661074.
10. Buchan, J. R.,, L. S. Aucott, and, I. Stansfield. 2006. tRNA properties help shape codon pair preferences in open reading frames. Nucleic Acids Res. 34:10151027.
11. Reference deleted.
12. Burns, C. C.,, R. Campagnoli,, J. Shaw,, A. Vincent,, J. Jorba, and, O. Kew. 2009. Genetic inactivation of poliovirus infectivity by increasing the frequencies of CpG and UpA dinucleotides within and across synonymous capsid region codons. J. Virol. 83:99579969.
13. Burns, C. C.,, J. Shaw,, R. Campagnoli,, J. Jorba,, A. Vincent,, J. Quay, and, O. Kew. 2006. Modulation of poliovirus replicative fitness in HeLa cells by deoptimization of synonymous codon usage in the capsid region. J. Virol. 80:32593272.
14. Caballero, S.,, S. Guix,, W. M. El Senousy,, I. Calico,, R. M. Pinto, and, A. Bosch. 2003. Persistent gastroenteritis in children infected with astrovirus: association with serotype-3 strains. J. Med. Virol. 71:245250.
15. Cello, J.,, A. V. Paul, and, E. Wimmer. 2002. Chemical synthesis of poliovirus cDNA: generation of infectious virus in the absence of natural template. Science 297:10161018.
16. Chan, M. C. W.,, J. J. Y. Sung,, R. K. Y. Lam,, P. K. S. Chan,, N. L. S. Lee,, R. W. M. Lai, and, W. K. Leung. 2006. Fecal viral load and norovirus-associated gastroenteritis. Emerg. Infect. Dis. 12:12781280.
17. Chiapello, H.,, F. Lisacek,, M. Caboche, and, H. Alain. 1998. Codon usage and gene function are related in sequences of Arabidopsis thaliana. Gene 209:GC1GC38.
18. Coleman, J. R.,, D. Papamichail,, S. Skiena,, B. Futcher,, E. Wimmer, and, S. Mueller. 2008. Virus attenuation by genome-scale changes in codon pair bias. Science 320:17841787.
19. Costafreda, M. I.,, A. Bosch, and, R. M. Pinto. 2006. Development, evaluation, and standardization of a real-time TaqMan reverse transcription-PCR assay for quantification of hepatitis A virus in clinical and shellfish samples. Appl. Environ. Microbiol. 72:38463855.
20. Curran, J. F.,, E. S. Poole,, W. P. Tate, and, B. L. Gross. 1995. Selection of aminoacyl-tRNAs at sense codons: the size of the tRNA variable loop determines whether the immediate 3′ nucleotide to the codon has a context effect. Nucleic Acids Res. 23:41044108.
21. Dentinger, C. M.,, W. A. Bower,, O. V. Nainan,, S. M. Cotter,, G. Myers,, L. M. Dubusky,, S. Fowler,, E. D. Salehi, and, B. P. Bell. 2001. An outbreak of hepatitis A associated with green onions. J. Infect. Dis. 183:12731276.
22. Ehrenfeld, E., and, N. L. Teterina. 2002. Initiation of translation of picornavirus RNAs: structure and function of the internal ribosome entry site, p. 159–169. In B. L. Semler and, E. Wimmer (ed.), Molecular Biology of Picornaviruses. ASM Press, Washington, DC.
23. Fedorov, A.,, S. Saxonov, and, W. Gilbert. 2002. Regularities of context-dependent codon bias in eukaryotic genes. Nucleic Acids Res. 30:11921197.
24. Gavrilin, G. V.,, E. A. Cherkasova,, G. Y. Lipskaya,, O. M. Kew, and, V. I. Agol. 2000. Evolution of circulating wild poliovirus and vaccine-derived poliovirus in an immunodeficient patient: a unifying model. J. Virol. 74:73817390.
25. Geller, R.,, M. Vignuzzi,, R. Andino, and, J. Frydman. 2007. Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev. 21:195205.
26. Grantham, R.,, C. Gautier, and, M. Gouy. 1980. Codon frequencies in 119 individual genes confirm consistent choices of degenerate bases according to genome type. Nucleic Acids Res. 8:18931912.
27. Grantham, R.,, C. Gautier,, M. Gouy,, R. Mercier, and, A. Pave. 1980. Codon catalog usage and the genome hypothesis. Nucleic Acids Res. 8:R49R62.
28. Gutman, G. A., and, G. W. Hatfield. 1989. Nonrandom utilization of codon pairs in Escherichia coli. Proc. Natl. Acad. Sci. USA 86:36993703.
29. Hollinger, F. B., and, S. U. Emerson. 2007. Hepatitis A virus, p. 911–947. In D. M. Knipe and, P. M. Howley (ed.), Fields Virology, 5th ed. Lippincott Williams and Wilkins, Philadelphia, PA.
30. Ikemura, T. 1981. Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes. J. Mol. Biol. 146:121.
31. Irwin, B.,, J. D. Heck, and, G. W. Hatfield. 1995. Codon pair utilization biases influence translational elongation step times. J. Biol. Chem. 270:2280122806.
32. Jackson, T. A. 2002. Proteins involved in the function of picornavirus internal ribosome entry sites, p. 171–186. In B. L. Semler and, E. Wimmer (ed.), Molecular Biology of Picornaviruses. ASM Press, Washington, DC.
33. Jansen, R. W.,, J. E. Newbold, and, S. M. Lemon. 1988. Complete nucleotide sequence of a cell culture-adapted variant of hepatitis a virus: comparison with wild-type virus with restricted capacity for in vitro replication. Virology 163:299307.
34. Joklik, W. K., and, J. E. Darnell, Jr. 1961. The adsorption and early fate of purified poliovirus in HeLa cells. Virology 13:439447.
35. Karlin, S.,, B. E. Blaisdell, and, G. A. Schachtel. 1990. Contrasts in codon usage of latent versus productive genes of Epstein-Barr virus: data and hypotheses. J. Virol. 64:42644273.
36. Koike, S.,, C. Taya,, T. Kurata,, S. Abe,, I. Ise,, H. Yonekawa, and, A. Nomoto. 1991. Transgenic mice susceptible to poliovirus. Proc. Natl. Acad. Sci. USA 88:951955.
37. Kuechler, E.,, J. Seipelt,, H.-D. Liebig, and, W. Sommergruber. 2002. Picornavirus proteinase-mediated shutoff of host cell translation: direct cleavage of a cellular initiation factor, p. 301–312. In B. L. Semler and, E. Wimmer (ed.), Molecular Biology of Picornaviruses. ASM Press, Washington, DC.
38. Laassri, M.,, K. Lottenbach,, R. Belshe,, M. Wolff,, M. Rennels,, S. Plotkin, and, K. Chumakov. 2005. Effect of different vaccination schedules on excretion of oral poliovirus vaccine strains. J. Infect. Dis. 192:20922098.
39. Lemon, S. M., and, B. H. Robertson. 1993. Current perspectives in the virology and molecular-biology of hepatitis A virus. Semin. Virol. 4:285295.
40. Leong, L. E. C.,, C. T. Cornell, and, B. L. Semler. 2002. Processing determinants and functions of cleavage products of picornavirus, p. 187–198. In B. L. Semler and, E. Wimmer (ed.), Molecular Biology of Picornaviruses. ASM Press, Washington, DC.
41. Marin, M. 2008. Folding at the rhythm of the rare codon beat. J. Biotechnol. 3:10471057.
42. Mbithi, J. N.,, V. S. Springthorpe, and, S. A. Sattar. 1991. Effect of relative humidity and air temperature on survival of hepatitis A virus on environmental surfaces. Appl. Environ. Microbiol. 57:13941399.
43. Moriyama, E. N., and, J. R. Powell. 1997. Codon usage bias and tRNA abundance in Drosophila. J. Mol. Evol. 45:514523.
44. Moura, G.,, M. Pinheiro,, R. Silva,, I. Miranda,, V. Afreixo,, G. Dias,, A. Freitas,, J. L. Oliveira, and, M. A. Santos. 2005. Comparative context analysis of codon pairs on an ORFeome scale. Genome Biol. 6:R28.
45. Mueller, S.,, D. Papamichail,, J. R. Coleman,, S. Skiena, and, E. Wimmer. 2006. Reduction of the rate of poliovirus protein synthesis through large-scale codon deoptimization causes attenuation of viral virulence by lowering specific infectivity. J. Virol. 80:96879696.
46. Musto, H.,, S. Cruveiller,, G. D’Onofrio,, H. Romero, and, G. Bernardi. 2001. Translational selection on codon usage in Xenopus laevis. Mol. Biol. Evol. 18:17031707.
47. Pallansch, M., and, R. Roos. 2007. Enteroviruses: polioviruses, coxsackieviruses, echoviruses, and newer enteroviruses, p. 839–893. In D. M. Knipe and, P. M. Howley (ed.), Fields Virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
48. Park, S.,, X. Yang, and, J. G. Saven. 2004. Advances in computational protein design. Curr. Opin. Struct. Biol. 14:487494.
49. Pinto, R. M.,, S. Guix,, J. F. Gonzalez-Dankaart,, S. Caballero,, G. Sanchez,, K. J. Guo,, E. Ribes, and, A. Bosch. 2002. Hepatitis A virus polyprotein processing by Escherichia coli proteases. J. Gen. Virol. 83:359368.
50. Reich, E.,, R. M. Franklin,, A. J. Shatkin, and Tatumel. 1962. Action of actinomycin D on animal cells and viruses. Proc. Natl. Acad. Sci. USA 48:12381245.
51. Reid, T. M. S., and, H. G. Robinson. 1987. Frozen raspberries and hepatitis A. Epidemiol. Infect. 98:109112.
52. Rosemblum, L. S.,, I. R. Mirkin,, D. T. Allen,, S. Safford, and, S. C. Hadler. 1990. A multistate outbreak of hepatitis A traced to commercially distributed lettuce. Am. J. Public Health 80:10751080.
53. Sanchez, G.,, A. Bosch, and, R. M. Pinto. 2003. Genome variability and capsid structural constraints of hepatitis A virus. J. Virol. 77:452459.
54. Sanchez, G.,, R. M. Pinto,, H. Vanaclocha, and, A. Bosch. 2002. Molecular characterization of hepatitis a virus isolates from a transcontinental shellfish-borne outbreak. J. Clin. Microbiol. 40:41484155.
55. Schwerdt, C. E., and, J. Fogh. 1957. The ratio of physical particles per infectious unit observed for poliomyelitis viruses. Virology 4:4152.
56. Sobsey, M. D.,, P. A. Shields,, F. S. Hauchman,, A. L. Davies,, V. A. Rullman, and, A. Bosch. 1988. Survival and persistence of hepatitis A virus in environmental samples, p. 121–124. In A. J. Zuckerman (ed.), Viral Hepatitis and Liver Disease. Alan R. Liss, Inc., New York, NY.
57. Stenico, M.,, A. T. Lloyd, and, P. M. Sharp. 1994. Codon usage in Caenorhabditis elegans: delineation of translational selection and mutational biases. Nucleic Acids Res. 22:24372446.
58. Sugiyama, T.,, M. Gursel,, F. Takeshita,, C. Coban,, J. Conover,, T. Kaisho,, S. Akira,, D. M. Klinman, and, K. J. Ishii. 2005. CpG RNA: identification of novel single-stranded RNA that stimulates human CD14+CD11c+ monocytes. J. Immunol. 174:22732279.
59. Takeshita, F.,, I. Gursel,, K. J. Ishii,, K. Suzuki,, M. Gursel, and, D. M. Klinman. 2004. Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9. Semin. Immunol. 16:1722.
60. Tucker, K. L. 2001. Methylated cytosine and the brain: a new base for neuroscience. Neuron 30:649652.
61. Whetter, L. E.,, S. P. Day,, O. Elroystein,, E. A. Brown, and, S. M. Lemon. 1994. Low efficiency of the 5′ nontranslated region of hepatitis A virus RNA in directing cap-independent translation in permissive monkey kidney cells. J. Virol. 68:52535263.
62. Wright, F. 1990. The effective number of codons used in a gene. Gene 87:2329.
63. Yang, Z., and, R. Nielsen. 2008. Mutation-selection models of codon substitution and their use to estimate selective strengths on codon usage. Mol. Biol. Evol. 25:568579.
64. Zhang, G., and, Z. Ignatova. 2009. Generic algorithm to predict the speed of translational elongation: implications for protein biogenesis. PLoS One 4:e5036.
65. Zhou, J.,, W. J. Liu,, S. W. Peng,, X. Y. Sun, and, I. Frazer. 1999. Papillomavirus capsid protein expression level depends on the match between codon usage and tRNA availability. J. Virol. 73:49724982.
66. Zhou, T.,, M. Weems, and, C. O. Wilke. 2009. Translationally optimal codons associate with structurally sensitive sites in proteins. Mol. Biol. Evol. 26:15711580.

Tables

Generic image for table
Table 1.

Dinucleotide statistics in poliovirus, hepatitis A virus, and various synthetic poliovirus capsid coding sequences

Citation: Bosch A, Mueller S, Pintó R. 2010. Coding Biases and Viral Fitness, p 271-283. In Ehrenfeld E, Domingo E, Roos R (ed), The Picornaviruses. ASM Press, Washington, DC. doi: 10.1128/9781555816698.ch17

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