M148R and M149R are two virulence factors for myxoma virus pathogenesis in the European rabbit

Veterinary Research

Volumn 40, Issue 1, 2009, Pages

  Blanié, Sophie ^a,b   Mortier, Jérémy ^a,b   Delverdier, Maxence ^a,b   Bertagnoli, Stéphane ^a,b   Camus Bouclainville, Christelle ^a,b  

^a IHAP   (France)

^b UNIVERSITÉ DE TOULOUSE   (France)

Author keywords

Ankyrin repeat; Myxoma virus; Poxvirus; Rabbit; Virulence

Indexed keywords

ANKYRIN; F BOX PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; PROTEIN M148R; PROTEIN M149R; UNCLASSIFIED DRUG; VIRULENCE FACTOR; VIRUS PROTEIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOPLASM; EUROPE; GENE DELETION; GENE TARGETING; HISTOPATHOLOGY; IN VITRO STUDY; IN VIVO STUDY; MYXOMA; MYXOMA VIRUS; NONHUMAN; NUCLEOLUS; PATHOGENESIS; PATHOGENICITY; PROTEIN ANALYSIS; PROTEIN MOTIF; RABBIT; VIRUS STRAIN; VIRUS VIRULENCE; ANIMAL; CELL LINE; CHEMISTRY; GENE EXPRESSION REGULATION; GENETICS; MALE; METABOLISM; MYXOMATOSIS; PHYSIOLOGY; VIROLOGY; VIRUS LOAD; VIRUS REPLICATION;

MYXOMA VIRUS; ORYCTOLAGUS CUNICULUS; POXVIRIDAE; PRIMATES;

ANIMALS; ANKYRIN REPEAT; CELL LINE; F-BOX PROTEINS; GENE EXPRESSION REGULATION, VIRAL; MALE; MYXOMA VIRUS; MYXOMATOSIS, INFECTIOUS; RABBITS; VIRAL LOAD; VIRAL PROTEINS; VIRULENCE FACTORS; VIRUS REPLICATION;

EID: 58249116641     PISSN: 09284249     EISSN: 12979716     Source Type: Journal    
DOI: 10.1051/vetres:2008049     Document Type: Article

References (35)

1. Andrade M.A., Ponting C.P., Gibson T.J., Bork P., Homology-based method for identification of protein repeats using statistical significance estimates, J. Mol. Biol. (2000) 298:521-537.
2. Bork P., Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?, Proteins (1993) 17:363-374.
3. Bradley R.R., Terajima M., Vaccinia virus K1L protein mediates host-range function in RK-13 cells via ankyrin repeat and may interact with a cellular GTPase-activating protein, Virus Res. (2005) 114:104-112.
4. Broyles S.S., Vaccinia virus transcription, J. Gen. Virol. (2003) 84:2293-2303.
5. Cameron C., Hota-Mitchell S., Chen L., Barrett J., Cao J.X., Macaulay C., et al., The complete DNA sequence of myxoma virus, Virology (1999) 264:298-318.
6. Camus-Bouclainville C., Fiette L., Bouchiha S., Pignolet B., Counor D., Filipe C., et al., A virulence factor of myxoma virus colocalizes with NF-kappaB in the nucleus and interferes with inflammation, J. Virol. (2004) 78:2510-2516.
7. Chakrabarti S., Brechling K., Moss B., Vaccinia virus expression vector: coexpression of beta-galactosidase provides visual screening of recombinant virus plaques, Mol. Cell. Biol. (1985) 5:3403-3409.
8. Dundr M., Leno G.H., Hammarskjold M.L., Rekosh D., Helga-Maria C., Olson M.O., The roles of nucleolar structure and function in the subcellular location of the HIV-1 Rev protein, J. Cell Sci. (1995) 108:2811-2823.
9. Falkner F.G., Moss B., Transient dominant selection of recombinant vaccinia viruses, J. Virol. (1990) 64:3108-3111.
10. Fankhauser C., Izaurralde E., Adachi Y., Wingfield P., Laemmli U.K., Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element, Mol. Cell. Biol. (1991) 11:2567-2575.
11. Finn R.D., Tate J., Mistry J., Coggill P.C., Sammut S.J., Hotz H.R., et al., The Pfam protein families database, Nucleic Acids Res. (2008) 36:D281-288.
12. Jin J., Cardozo T., Lovering R.C., Elledge S.J., Pagano M., Harper J.W., Systematic analysis and nomenclature of mammalian F-box proteins, Genes Dev. (2004) 18:2573-2580.
13. Jin J., Ang X.L., Shirogane T., Wade Harper J., Identification of substrates for F-box proteins, Methods Enzymol. (2005) 399:287-309.
14. Letunic I., Copley R.R., Pils B., Pinkert S., Schultz J., Bork P., SMART 5: domains in the context of genomes and networks, Nucleic Acids Res. (2006) 34:D257-D260.
15. Marck C., 'DNA Strider': a 'C' program for the fast analysis of DNA and protein sequences on the Apple Macintosh family of computers, Nucleic Acids Res. (1988) 16:1829-1836.
16. Mears W.E., Lam V., Rice S.A., Identification of nuclear and nucleolar localization signals in the herpes simplex virus regulatory protein ICP27, J. Virol. (1995) 69:935-947.
17. Mercer A.A., Fleming S.B., Ueda N., F-box-like domains are present in most poxvirus ankyrin repeat proteins, Virus Genes (2005) 31:127-133.
18. Mossman K., Lee S.F., Barry M., Boshkov L., McFadden G., Disruption of M-T5, a novel myxoma virus gene member of poxvirus host range superfamily, results in dramatic attenuation of myxomatosis in infected European rabbits, J. Virol. (1996) 70:4394-4410.
19. Olson M.O., Dundr M., Szebeni A., The nucleolus: an old factory with unexpected capabilities, Trends Cell Biol. (2000) 10:189-196.
20. Olson M.O., Hingorani K., Szebeni A., Conventional and nonconventional roles of the nucleolus, Int. Rev. Cytol. (2002) 219:199-266.
21. Pederson T., The plurifunctional nucleolus, Nucleic Acids Res. (1998) 26:3871-3876.
22. Perkus M.E., Goebel S.J., Davis S.W., Johnson G.P., Limbach K., Norton E.K., Paoletti E., Vaccinia virus host range genes, Virology (1990) 179:276-286.
23. Pignolet B., Boullier S., Gelfi J., Bozzetti M., Russo P., Foulon E., et al., Safety and immunogenicity of myxoma virus as a new viral vector for small ruminants, J. Gen. Virol. (2008) 89:1371-1379.
24. Sachdev S., Hoffmann A., Hannink M., Nuclear localization of IkappaB alpha is mediated by the second ankyrin repeat: the IkappaB alpha ankyrin repeats define a novel class of cis-acting nuclear import sequences, Mol. Cell. Biol. (1998) 18:2524-2534.
25. Shisler J.L., Jin X.L., The vaccinia virus K1L gene product inhibits host NF-kappaB activation by preventing IkappaBalpha degradation, J. Virol. (2004) 78:3553-3560.
26. Siomi H., Shida H., Maki M., Hatanaka M., Effects of a highly basic region of human immunodeficiency virus Tat protein on nucleolar localization, J. Virol. (1990) 64:1803-1807.
27. Sonnberg S., Seet B.T., Pawson T., Fleming S.B., Mercer A.A., Poxvirus ankyrin repeat proteins are a unique class of F-box proteins that associate with cellular SCF1 ubiquitin ligase complexes, Proc. Natl. Acad. Sci. USA (2008) 105:10955-10960.
28. Sperling K.M., Schwantes A., Schnierle B.S., Sutter G., The highly conserved orthopoxvirus 68k ankyrin-like protein is part of a cellular SCF ubiquitin ligase complex, Virology (2008) 374:234-239.
29. Stanford M.M., Werden S.J., McFadden G., Myxoma virus in the European rabbit: interactions between the virus and its susceptible host, Vet. Res. (2007) 38:299-318.
30. Szekely L., Jiang W.Q., Pokrovskaja K., Wiman K.G., Klein G., Ringertz N., Reversible nucleolar translocation of Epstein-Barr virus-encoded EBNA-5 and hsp70 proteins after exposure to heat shock or cell density congestion, J. Gen. Virol. (1995) 76:2423-2432.
31. Upton C., Macen J.L., McFadden G., Mapping and sequencing of a gene from myxoma virus that is related to those encoding epidermal growth factor and transforming growth factor alpha, J. Virol. (1987) 61:1271-1275.
32. Upton C., Macen J.L., Maranchuk R.A., DeLange A.M., McFadden G., Tumorigenic poxviruses: fine analysis of the recombination junctions in malignant rabbit fibroma virus, a recombinant between Shope fibroma virus and myxoma virus, Virology (1988) 166:229-239.
33. Werden S.J., Barrett J.W., Wang G., Stanford M.M., McFadden G., M-T5, the ankyrin repeat, host range protein of myxoma virus, activates Akt and can be functionally replaced by cellular PIKE-A, J. Virol. (2007) 81:2340-2348.
34. Werden S.J., McFadden G., The role of cell signaling in poxvirus tropism: the case of the MT5 host range protein of myxoma virus, Biochim. Biophys. Acta (2008) 1784:228-237.
35. Wheeler D.L., Barrett T., Benson D.A., Bryant S.H., Canese K., Chetvernin V., et al., Database resources of the National Center for Biotechnology Information, Nucleic Acids Res. (2008) 36:D13-D21.