Phosphorylation of dGMP analogs by vaccinia virus TMP kinase and human GMP kinase

Biochemical and Biophysical Research Communications

Volumn 388, Issue 1, 2009, Pages 6-11

  Auvynet, Constance ^a   Topalis, Dimitri ^a   Caillat, Christophe ^b   Munier Lehmann, Hélène ^c   Seclaman, Edward ^c   Balzarini, Jan ^d   Agrofoglio, Luigi André ^e   Kaminski, Pierre Alexandre ^c   Meyer, Philippe ^b   Deville Bonne, Dominique ^a   El Amri, Chahrazade ^a  

^a SORBONNE UNIVERSITÉ   (France)

^b LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

^c CNRS   (France)

^d REGA INSTITUTE FOR MEDICAL RESEARCH   (Belgium)

^e UNIVERSITÉ D'ORLÉANS   (France)

Author keywords

8 oxo dGMP; 9 deaza dGMP; Alkylated dGMP; Glyoxal dGMP; GMP kinase; O6 Me dGMP; Phosphorylation; TMP kinase; Vaccinia virus

Indexed keywords

DEOXYGUANOSINE PHOSPHATE; GUANYLATE KINASE; O 6 METHYLDEOXYGUANOSINE MONOPHOSPHATE; THYMIDYLATE KINASE; UNCLASSIFIED DRUG; VIRUS ENZYME;

ARTICLE; ENZYME ACTIVITY; ENZYME STRUCTURE; MOLECULAR DOCKING; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; VACCINIA VIRUS;

ANTIVIRAL AGENTS; DEOXYGUANINE NUCLEOTIDES; DRUG DESIGN; GUANYLATE KINASE; HUMANS; NUCLEOSIDE-PHOSPHATE KINASE; PHOSPHORYLATION; SUBSTRATE SPECIFICITY; VACCINIA VIRUS;

VACCINIA VIRUS;

EID: 68949154434     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.07.089     Document Type: Article

References (40)

1. Georges A.J., Matton T., and Courbot-Georges M.C. Monkeypox, a model of emergent then reemergent disease. Med. Mal. Infect. 34 (2004) 12-19
2. Smith S., Olson V., Karem K., Jordan R., Hruby D., and Damon I. In vitro efficacy of ST246 against smallpox and monkeypox. Antimicrob. Agents Chemother. 53 (2009) 1007-1012
3. Becker M., Obraztsova M., Kern E., Quenelle D., Keith K., Prichard M.N., Luo M., and Moyer R. Isolation and characterization of cidofovir resistant vaccinia viruses. Virol. J. 14 (2008) 58-65
4. Assarsson E., Greenbaum J.A., Sundstrom M., Schaffer L., Hammond J.A., Pasquetto V., Oseroff C., Hendrickson R.C., Lefkowitz E.J., Tscharke D.C., Sidney J., Grey H.M., Head S.R., Peters B., and Sette A. Kinetic analysis of a complete poxvirus transcriptome reveals an immediate-early class of genes. Proc. Natl. Acad. Sci. USA 105 (2008) 2140-2145
5. Smith G.L., de Carlos A., and Chan Y.S. Vaccinia virus encodes a thymidylate kinase gene: sequence and transcriptional mapping. Nucl. Acids Res. 17 (1989) 7581-7590
6. El Omari K., Solaroli N., Karlsson A., Balzarini J., and Stammers D.K. Structure of vaccinia virus thymidine kinase in complex with dTTP: insights for drug design. BMC Struct. Biol. 6 (2006) 22-31
7. Solaroli N., Johansson M., Balzarini J., and Karlsson A. Substrate specificity of three viral thymidine kinases (TK): vaccinia virus TK, feline herpesvirus TK, and canine herpesvirus TK. Nucleosides Nucleotides Nucleic Acids 25 (2006) 1189-1192
8. Topalis D., Collinet B., Gasse C., Dugue L., Balzarini J., Pochet S., and Deville-Bonne D. Substrate specificity of vaccinia virus thymidylate kinase. FEBS J. 272 (2005) 6254-6265
9. Caillat C., Topalis D., Agrofoglio L.A., Pochet S., Balzarini J., Deville-Bonne D., and Meyer P. Crystal structure of poxvirus thymidylate kinase: a dimerization with implications for antiviral therapy. Proc. Natl. Acad. Sci. USA 105 (2008) 16900-16905
10. Fyfe J.A. Differential phosphorylation of (E)-5-(2-bromovinyl)-2′-deoxyuridine monophosphate by thymidylate kinases from herpes simplex viruses types 1 and 2 and varicella zoster virus. Mol. Pharmacol. 21 (1982) 432-437
11. De Clercq E. Discovery and development of BVDU (brivudin) as a therapeutic for the treatment of herpes zoster. Biochem. Pharmacol. 68 (2004) 2301-2315
12. Thorne S.H., Hwang T.H., O'Gorman W.E., Bartlett D.L., Sei S., Kanji F., Brown C., Werier J., Cho J.H., Lee D.E., Wang Y., Bell J., and Kirn D.H. Rational strain selection and engineering creates a broad-spectrum, systemically effective oncolytic poxvirus, JX-963. J. Clin. Invest. 117 (2007) 3350-3358
13. Murata-Kamiya N., Kamiya H., Kaji H., and Kasai H. Glyoxal, a major product of DNA oxidation, induces mutations at G:C sites on a shuttle vector plasmid replicated in mammalian cells. Nucleic Acids Res. 25 (1997) 1897-1902
14. Cooke M.S., and Evans M.D. 8-Oxo-deoxyguanosine: reduce, reuse, recycle?. Proc. Natl. Acad. Sci. USA 104 (2007) 13535-13536
15. Kaina B., Christmann M., Naumann S., and Roos W.P. MGMT: key node in the battle against genotoxicity, carcinogenicity and apoptosis induced by alkylating agents. DNA Repair (Amst) 6 (2007) 1079-1099
16. Ghiorghi Y.K., Zeller K.I., Dang C.V., and Kaminski P.A. The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5′-monophosphate N-glycosidase. J. Biol. Chem. 282 (2007) 8150-8156
17. Pochet S., Dugué L., Labesse G., Delepierre M., and Munier-Lehmann H. Comparative study of purine and pyrimidine nucleoside analogs acting on the thymidylate kinases of Mycobacterium tuberculosis and of humans. Chembiochem 4 (2003) 742-747
18. Sambrook J., Fritsch E.F., and Manniatis T. Molecular Cloning: A Laboratory Manual (1989), Cold Spring harbour, New York, USA
19. Sanger F., Nicklen S., and Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74 (1977) 5463-5467
20. Blondin C., Serina L., Wiesmuller L., Gilles A.-M., and Barzu O. Improved spectrophotometric assay of nucleoside monophosphate kinase activity using the pyruvate kinase/lactate dehydrogenase coupling system. Anal. Biochem. 220 (1994) 219-221
21. Schuettelkopf A., and Van Alten D. PRODRG, a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D60 (2004) 1355-1363
22. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges N., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Crystallography and NMR system (CNS): a new software system for macromolecular structure determination. Acta Cryst. D54 (1998) 905-921
23. Eswar N., Marti-Renom A., Webb B., Madhusudhan M., Eramian D., Shen M., Pieper U., and Sali A. Current Protocols in Bioinformatics (2004), John Wiley & Sons, Inc. pp. 5.6.1-5.6.30
24. Brady W., Kokoris M., Fitzgibbon M., and Black M. Cloning, characterization, and modeling of mouse and human guanylate kinases. J. Biol. Chem. 271 (1996) 16734-16740
25. Prinz H., Lavie A., Scheidig A., Spangenberg O., and Konrad M. Binding of nucleotides to guanylate kinase, p21ras, and nucleoside-diphosphate kinase studied by nano-electrospray mass spectrometry. J. Biol. Chem. 274 (1999) 35337-35342
26. Li Y., Zhang Y., and Yan H. Kinetic and thermodynamic characterizations of yeast guanylate kinase. J. Biol. Chem. 271 (1996) 28038-28044
27. Boehme R. Phosphorylation of the antiviral precursor 9-(1,3-dihydroxy-2-propoxymethyl)guanine monophosphate by guanylate kinase isozymes. J. Biol. Chem. 259 (1984) 12346-12349
28. Krejcova R., Horska K., Votruba I., and Holy A. Interaction of guanine phosphonomethoxyalkyl derivatives with GMP kinase isoenzymes. Biochem. Pharmacol. 60 (2000) 1907-1913
29. Topalis D., Alvarez K., Barral K., Munier-Lehmann H., Schneider B., Véron M., Guerreiro C., Mulard L., El-Amri C., Canard B., and Deville-Bonne D. Acyclic phosphonate nucleotides and human adenylate kinases: impact of a borano group on alpha-P position. Nucleosides Nucleotides Nucleic Acids 27 (2008) 319-331
30. Hah S.S., Mundt J.M., Kim H.M., Sumbad R.A., Turteltaub K.W., and Henderson P.T. Measurement of 7,8-dihydro-8-oxo-2′-deoxyguanosine metabolism in MCF-7 cells at low concentrations using accelerator mass spectrometry. Proc. Natl. Acad. Sci. USA 104 (2007) 11203-11208
31. Blaszczyk J., Li Y., Yan H., and Ji X. Crystal structure of unligated guanylate kinase from yeast reveals GMP-induced conformational changes. J. Mol. Biol. 307 (2001) 247-257
32. Ardiani A., Goyke A., and Black M. Mutations at serine 37 in mouse guanylate kinase confer resistance to 6-thioguanine. Protein Eng. Des. Sel. 22 (2009) 225-232
33. Sekiguchi M., and Tsuzuki T. Oxidative nucleotide damage: consequences and prevention. Oncogene 21 (2002) 8895-8904
34. Hayakawa H., Hofer A., Thelander L., Kitajima S., Cai Y., Oshiro S., Yakushiji H., Nakabeppu Y., Kuwano M., and Sekiguchi M. Metabolic fate of oxidized guanine ribonucleotides in mammalian cells. Biochemistry 38 (1999) 3610-3614
35. Lascu I., and Gonin P. The catalytic mechanism of nucleoside diphosphate kinases. J. Bioenerg. Biomembr. 32 (2000) 237-246
36. Vaca C.E., Fang J.L., Conradi M., and Hou S.M. Development of a 32P-postlabelling method for the analysis of 2′-deoxyguanosine-3′-monophosphate and DNA adducts of methylglyoxal. Carcinogenesis 15 (1994) 1887-1894
37. Eadie J., Conrad M., Toorchen D., and Topal M. Mechanism of mutagenesis by O6-methylguanine. Nature 308 (1984) 201-203
38. Lemoine E., Mesel-Lemoine M., Cherai M., Gallot G., Vié H., Leclercq V., Trebeden-Negre H., Mammes O., Boyer O., Noguiez-Hellin P., and LKlatzmann D. Efficient transduction and selection of human T-lymphocytes with bicistronic Thy1/HSV1-TK retroviral vector produced by a human packaging cell line. J. Gene Med. 6 (2004) 374-386
39. Meier C., and Balzarini J. Application of the cycloSal-prodrug approach for improving the biological potential of phosphorylated biomolecules. Antiviral. Res. 71 (2006) 282-292
40. Cahard D., McGuigan C., and Balzarini J. Aryloxy phosphoramidate triesters as pro-tides. Mini-Rev. Med. Chem. 4 (2004) 371-382