Quantitative evaluation of viral fitness due to a single nucleotide polymorphism in the Marek's disease virus UL41 gene via an in vitro competition assay

Journal of Virological Methods

Volumn 148, Issue 1-2, 2008, Pages 125-131

  Mao, Weifeng ^a,b   Niikura, Masahiro ^b,c   Silva, Robert F ^b   Cheng, Hans H ^b  

^a MICHIGAN STATE UNIVERSITY   (United States)

^b AGRICULTURAL RESEARCH SERVICE   (United States)

^c NONE   (United States)

Author keywords

Fitness; Marek's disease virus; Polymorphism; Pyrosequencing; Virion host shutoff gene

Indexed keywords

ALLELE; ARTICLE; BACTERIAL ARTIFICIAL CHROMOSOME; BIRD DISEASE; CONTROLLED STUDY; ENZYME ACTIVITY; GENE FUNCTION; IN VITRO STUDY; MARDIVIRUS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PYROSEQUENCING; QUANTITATIVE ANALYSIS; SINGLE NUCLEOTIDE POLYMORPHISM; UL41 GENE; VIROGENESIS; VIRULENCE; VIRUS GENE;

AMINO ACID SUBSTITUTION; ANIMALS; CHICK EMBRYO; HERPESVIRUS 2, GALLID; PLAQUE ASSAY; POLYMORPHISM, SINGLE NUCLEOTIDE; VIRAL PROTEINS; VIROLOGY; VIRULENCE;

BACTERIA (MICROORGANISMS); GALLID HERPESVIRUS 2; GALLUS GALLUS;

EID: 39149131379     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jviromet.2007.10.024     Document Type: Article

References (37)

1. Barzilai A., Zivony-Elbom I., Sarid R., Noah E., and Frenkel N. The herpes simplex virus type 1 vhs-UL41 gene secures viral replication by temporarily evading apoptotic cellular response to infections with elements of cellular mRNA degradation machinery. J. Virol. 80 (2006) 505-513
2. Carrasco P., Daròs J.A., Agudelo-Romero P., and Elena S.F. A real-time RT-PCR assay for quantifying the fitness of tobacco etch virus in competition experiments. J. Virol. Meth. 139 (2007) 181-188
3. Costantino N., and Court D.L. Enhanced levels of λ Red-mediated recombinants in mismatch repair mutants. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 15748-15753
4. Court D.L., Swaminathan S., Yu D., Wilson H., Baker T., Bubunenko M., Sawitzke J., and Sharan S.K. Mini-λ: a tractable system for chromosome and BAC engineering. Gene 315 (2003) 63-69
5. Esclatine A., Taddeo B., and Roizman B. The UL41 protein of herpes simplex virus mediates selective stabilization or degradation of cellular mRNAs. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 18165-18170
6. Everly D.N., and Read G.S. Site-directed mutagenesis of the virion host shutoff gene (UL41) of herpes simplex virus (HSV): analysis of functional differences between HSV type 1 (HSV-1) and HSV-2 alleles. J. Virol. 73 (1999) 9117-9129
7. Geballe A.P., Spaete R.R., and Mocarski E.S. A cis-acting element within the 5′ leader of a cytomegalovirus B transcript determines kinetic class. Cell 46 (1986) 865-872
8. Himly M., Foster D.N., Bottoli I., Iacovoni J.S., and Vogt P.K. The DF-1 chicken fibroblast cell line: transformation induced by diverse oncogenes and cell death resulting from infection by avian leucosis viruses. Virology 248 (1998) 295-408
9. Holland J.J., de la Torre J.C., Clarke D.K., and Duarte E.A. Quantification of relative fitness and great adaptability of clonal populations of RNA viruses. J. Virol. 65 (1991) 2960-2967
10. Jones F.E., Smibert C.A., and Smiley J.R. Mutational analysis of the herpes simplex virus virion host shutoff protein: evidence that vhs functions in the absence of other viral proteins. J. Virol. 69 (1995) 4863-4871
11. Kamil J.P., Tischer B.K., Trapp S., Nair V.K., Osterrieder N., and Kung H.J. vLIP, a viral lipase homologue, is a virulence factor of Marek's disease virus. J. Virol. 79 (2005) 6984-6996
12. Kwong A.D., and Frenkel N. Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs. Proc. Natl. Acad. Sci. U.S.A. 84 (1987) 1926-1930
13. Kwong A.D., and Frenkel N. Herpes simplex virus virion host shutoff function. J. Virol. 62 (1988) 912-921
14. Lahser F.C., Wright-Minogue J., Skelton A., and Malcolm B.A. Quantitative estimation of viral fitness using pyrosequencing. BioTech 34 (2003) 26-28
15. Murphy J.A., Duerst R.J., Smith T.J., and Morrison L.A. Herpes simplex virus type 2 virion host shutoff protein regulates alpha/beta interferon but not adaptive immune responses during primary infection in vivo. J. Virol. 77 (2003) 9337-9345
16. Niikura M., Dodgson J., and Cheng H.H. Direct evidence of host genome acquisition by the alphaherpesvirus Marek's disease virus. Arch. Virol. 151 (2006) 537-549
17. Novella I.S. Contributions of vesicular stomatitis virus to the understanding of RNA virus evolution. Curr. Opin. Microbiol. 6 (2003) 399-405
18. O'Meara D., Wilbe K., Leitner T., Hejdeman B., Albert J., and Lundeberg J. Monitoring resistance to human innunodeficiency virus type 1 protease inhibitors by pyrosequencing. J. Clin. Microbiol. 39 (2001) 464-473
19. Osterrieder N., Kamil J.P., Schmacher D., Tischer B.K., and Trapp S. Marek's disease virus: from miasma to model. Nature Rev. Microbiol. 4 (2006) 283-294
20. Petherbridge L., Brown A.C., Baigent S.J., Howes K., Sacco M.A., Osterrieder N., and Nair V.K. Oncogenicity of virulent Marek's disease virus cloned as bacterial artificial chromosomes. J. Virol. 78 (2004) 13376-13380
21. Prigge J.T., Majerciak V., Hunt H.D., Dienglewicz R.L., and Parcells M.S. Construction and characterization of Marek's disease viruses having green fluorescent protein expression tied directly or indirectly to phosphoprotein 38 expression. Avian Dis. 48 (2004) 471-487
22. Read G.S., and Frenkel N. Herpes simplex virus mutants defective in the virion-associated shutoff polypeptide synthesis and exhibiting abnormal synthesis of α (immediate early) viral polypeptides. J. Virol. 46 (1983) 498-512
23. Read G.S., Karr B.M., and Knight K. Isolation of a herpes simplex virus type 1 mutant with a deletion in the virion host shutoff gene and identification of multiple forms of the vhs (UL41) polypeptide. J. Virol. 67 (1993) 7149-7160
24. Reddy S.M., Lupiani B., Gimeno I.M., Silva R.F., Lee L.F., and Witter R.L. Rescue of a pathogenic Marek's disease virus with overlapping cosmid DNAs: use of a pp38 mutant to validate the technology for the study of gene function. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 7054-7059
25. Ronaghi M. Pyrosequencing sheds light on DNA sequencing. Genome Res. 11 (2001) 3-11
26. Ronaghi M., Uhlen M., and Nyren P. A sequencing method based on real-time pyrophosphate. Science 281 (1998) 363-365
27. Schumacher D., Tischer B.K., Fuchs W., and Osterrieder N. Reconstitution of Marek's disease virus serotype 1 (MDV-1) from DNA cloned as a bacterial artificial chromosome and characterization of a glycoprotein B-negative MDV-1 mutant. J. Virol. 74 (2000) 11088-11098
28. Schumacher D., Tischer B.K., Trapp S., and Osterrieder N. The protein encoded by the US3 orthologue of Marek's disease virus is required for dfficient de-envelopment of perinuclear virions and involved in actin stress fiber breakdown. J. Virol. 79 (2005) 3987-3997
29. Silva R.F., Lee L.F., and Kutish G.F. The genomic structure of Marek's disease virus. In: Hirai K. (Ed). Marek's Disease (2001), Springer, Berlin 143-158
30. Silva R.F., Reddy S.M., and Lupiani B. Expansion of a unique region in the Marek's disease virus genome occurs concomitantly with attenuation but is not sufficient to cause attenuation. J. Virol. 78 (2004) 733-740
31. Smith T.J., Morrison L.A., and Leib D.A. Pathogenesis of herpes simplex virus type 2 virion host shutoff (vhs) mutants. J. Virol. 76 (2002) 2054-2061
32. Spatz S.J., and Silva R.F. Polymorphisms in the repeat long regions of oncogenic and attenuated pathotypes of Marek's disease virus 1. Virus Genes 35 (2007) 41-53
33. Spatz S.J., Peterbridge L., Zhao Y., and Nair V. Comparative full-length sequence analysis of oncogenic and vaccine (Rispens) strains of Marek's disease virus. J. Gen. Virol. 88 (2007) 1080-1096
34. Suzutani T., Nagamine M., Shibaki T., Ogasawara M., Yoshida I., Daikoku T., Nishiyama Y., and Azuma M. The role of the UL41 gene of herpes simplex virus type 1 in evasion of non-specific host defense mechanisms during primary infection. J. Gen. Virol. 81 (2000) 1763-1771
35. Taddeo B., and Roizman B. The virion host shutoff protein (UL41) of herpes simplex virus 1 is an endoribonuclease with a substrate specificity similar to that of RNase A. J. Virol. 80 (2006) 9341-9345
36. Witter R.L. Increased virulence of Marek's disease virus field isolates. Avian Dis. 41 (1996) 149-163
37. Yuste E., Bordería A.V., Domingo E., and López-Galíndez C. Few mutations in the 5′ leader region mediate fitness recovery of debilitated human immunodeficiency type 1viruses. J. Virol. 79 (2005) 5421-5427