Structures of NS5 Methyltransferase from Zika Virus

Cell Reports

Volumn 16, Issue 12, 2016, Pages 3097-3102

  Coloma, Javier ^a   Jain, Rinku ^a   Rajashankar, Kanagalaghatta R ^b,c   García Sastre, Adolfo ^a   Aggarwal, Aneel K ^a  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^b Cornell University ^*  (United States)

^c ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

7 METHYL GUANOSINE DIPHOSPHATE; ANTIVIRUS AGENT; GUANOSINE DIPHOSPHATE; METHYLTRANSFERASE; NONSTRUCTURAL PROTEIN 5 METHYLTRANSFERASE; S ADENOSYLMETHIONINE; S ADENOSYLMETHIONINE DERIVATIVE; UNCLASSIFIED DRUG; VIRUS RNA; VIRAL PROTEIN;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG RESEARCH; DRUG STRUCTURE; ENZYME ANALYSIS; ENZYME INHIBITOR COMPLEX; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN EXPRESSION; STRUCTURE ACTIVITY RELATION; ZIKA VIRUS; CHEMISTRY; ENZYMOLOGY; PROTEIN CONFORMATION;

METHYLTRANSFERASES; PROTEIN CONFORMATION; VIRAL NONSTRUCTURAL PROTEINS; ZIKA VIRUS;

EID: 84989870502     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2016.08.091     Document Type: Article

References (29)

1. Adams, P.D., Afonine, P.V., Bunkóczi, G., Chen, V.B., Davis, I.W., Echols, N., Headd, J.J., Hung, L.W., Kapral, G.J., Grosse-Kunstleve, R.W., et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66 (2010), 213–221.
2. Battye, T.G., Kontogiannis, L., Johnson, O., Powell, H.R., Leslie, A.G., iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM. Acta Crystallogr. D Biol. Crystallogr. 67 (2011), 271–281.
3. Benarroch, D., Egloff, M.P., Mulard, L., Guerreiro, C., Romette, J.L., Canard, B., A structural basis for the inhibition of the NS5 dengue virus mRNA 2′-O-methyltransferase domain by ribavirin 5′-triphosphate. J. Biol. Chem. 279 (2004), 35638–35643.
4. Bollati, M., Milani, M., Mastrangelo, E., Ricagno, S., Tedeschi, G., Nonnis, S., Decroly, E., Selisko, B., de Lamballerie, X., Coutard, B., et al. Recognition of RNA cap in the Wesselsbron virus NS5 methyltransferase domain: implications for RNA-capping mechanisms in Flavivirus. J. Mol. Biol. 385 (2009), 140–152.
5. Chen, H., Liu, L., Jones, S.A., Banavali, N., Kass, J., Li, Z., Zhang, J., Kramer, L.D., Ghosh, A.K., Li, H., Selective inhibition of the West Nile virus methyltransferase by nucleoside analogs. Antiviral Res. 97 (2013), 232–239.
6. Coutard, B., Decroly, E., Li, C., Sharff, A., Lescar, J., Bricogne, G., Barral, K., Assessment of Dengue virus helicase and methyltransferase as targets for fragment-based drug discovery. Antiviral Res. 106 (2014), 61–70.
7. Daigle, S.R., Olhava, E.J., Therkelsen, C.A., Majer, C.R., Sneeringer, C.J., Song, J., Johnston, L.D., Scott, M.P., Smith, J.J., Xiao, Y., et al. Selective killing of mixed lineage leukemia cells by a potent small-molecule DOT1L inhibitor. Cancer Cell 20 (2011), 53–65.
8. Davis, I.W., Leaver-Fay, A., Chen, V.B., Block, J.N., Kapral, G.J., Wang, X., Murray, L.W., Arendall, W.B. 3rd, Snoeyink, J., Richardson, J.S., Richardson, D.C., MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res., 35, 2007, W375-83.
9. Dong, H., Chang, D.C., Xie, X., Toh, Y.X., Chung, K.Y., Zou, G., Lescar, J., Lim, S.P., Shi, P.Y., Biochemical and genetic characterization of dengue virus methyltransferase. Virology 405 (2010), 568–578.
10. Dong, H., Fink, K., Züst, R., Lim, S.P., Qin, C.F., Shi, P.Y., Flavivirus RNA methylation. J. Gen. Virol. 95 (2014), 763–778.
11. Egloff, M.P., Benarroch, D., Selisko, B., Romette, J.L., Canard, B., An RNA cap (nucleoside-2′-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization. EMBO J. 21 (2002), 2757–2768.
12. Egloff, M.P., Decroly, E., Malet, H., Selisko, B., Benarroch, D., Ferron, F., Canard, B., Structural and functional analysis of methylation and 5′-RNA sequence requirements of short capped RNAs by the methyltransferase domain of dengue virus NS5. J. Mol. Biol. 372 (2007), 723–736.
13. Emsley, P., Cowtan, K., Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60 (2004), 2126–2132.
14. Fauci, A.S., Morens, D.M., Zika Virus in the Americas–Yet Another Arbovirus Threat. N. Engl. J. Med. 374 (2016), 601–604.
15. Kaniskan, H.U., Jin, J., Chemical probes of histone lysine methyltransferases. ACS Chem. Biol. 10 (2015), 40–50.
16. Lazear, H.M., Diamond, M.S., Zika Virus: New Clinical Syndromes and Its Emergence in the Western Hemisphere. J. Virol. 90 (2016), 4864–4875.
17. Li, S.H., Dong, H., Li, X.F., Xie, X., Zhao, H., Deng, Y.Q., Wang, X.Y., Ye, Q., Zhu, S.Y., Wang, H.J., et al. Rational design of a flavivirus vaccine by abolishing viral RNA 2′-O methylation. J. Virol. 87 (2013), 5812–5819.
18. Lim, S.P., Sonntag, L.S., Noble, C., Nilar, S.H., Ng, R.H., Zou, G., Monaghan, P., Chung, K.Y., Dong, H., Liu, B., et al. Small molecule inhibitors that selectively block dengue virus methyltransferase. J. Biol. Chem. 286 (2011), 6233–6240.
19. Luo, M., Current chemical biology approaches to interrogate protein methyltransferases. ACS Chem. Biol. 7 (2012), 443–463.
20. Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997), 307–326.
21. Panjikar, S., Parthasarathy, V., Lamzin, V.S., Weiss, M.S., Tucker, P.A., Auto-rickshaw: an automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment. Acta Crystallogr. D Biol. Crystallogr. 61 (2005), 449–457.
22. Petersen, L.R., Jamieson, D.J., Powers, A.M., Honein, M.A., Zika Virus. N. Engl. J. Med. 374 (2016), 1552–1563.
23. Ray, D., Shah, A., Tilgner, M., Guo, Y., Zhao, Y., Dong, H., Deas, T.S., Zhou, Y., Li, H., Shi, P.Y., West Nile virus 5′-cap structure is formed by sequential guanine N-7 and ribose 2′-O methylations by nonstructural protein 5. J. Virol. 80 (2006), 8362–8370.
24. Stahla-Beek, H.J., April, D.G., Saeedi, B.J., Hannah, A.M., Keenan, S.M., Geiss, B.J., Identification of a novel antiviral inhibitor of the flavivirus guanylyltransferase enzyme. J. Virol. 86 (2012), 8730–8739.
25. Wu, H., Min, J., Zeng, H., Plotnikov, A.N., Crystal structure of the methyltransferase domain of human TARBP1. Proteins 72 (2008), 519–525.
26. Yap, L.J., Luo, D., Chung, K.Y., Lim, S.P., Bodenreider, C., Noble, C., Shi, P.Y., Lescar, J., Crystal structure of the dengue virus methyltransferase bound to a 5′-capped octameric RNA. PLoS ONE, 5, 2010, e12836.
27. Zhao, Y., Soh, T.S., Lim, S.P., Chung, K.Y., Swaminathan, K., Vasudevan, S.G., Shi, P.Y., Lescar, J., Luo, D., Molecular basis for specific viral RNA recognition and 2′-O-ribose methylation by the dengue virus nonstructural protein 5 (NS5). Proc. Natl. Acad. Sci. USA 112 (2015), 14834–14839.
28. Zhou, Y., Ray, D., Zhao, Y., Dong, H., Ren, S., Li, Z., Guo, Y., Bernard, K.A., Shi, P.Y., Li, H., Structure and function of flavivirus NS5 methyltransferase. J. Virol. 81 (2007), 3891–3903.
29. Züst, R., Dong, H., Li, X.F., Chang, D.C., Zhang, B., Balakrishnan, T., Toh, Y.X., Jiang, T., Li, S.H., Deng, Y.Q., et al. Rational design of a live attenuated dengue vaccine: 2′-o-methyltransferase mutants are highly attenuated and immunogenic in mice and macaques. PLoS Pathog., 9, 2013, e1003521.