Effects of NS2B-NS3 protease and furin inhibition on West Nile and Dengue virus replication

Journal of Enzyme Inhibition and Medicinal Chemistry

Volumn 32, Issue 1, 2017, Pages 712-721

  Kouretova, Jenny ^a   Hammamy, M Zouhir ^a   Epp, Anton ^a   Hardes, Kornelia ^a   Kallis, Stephanie ^b   Zhang, Linlin ^c   Hilgenfeld, Rolf ^c   Bartenschlager, Ralf ^b   Steinmetzer, Torsten ^a  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

^b UNIVERSITY OF HEIDELBERG   (Germany)

^c UNIVERSITY OF LÜBECK   (Germany)

Author keywords

antiviral activity; Dengue virus; furin; NS2B NS3 protease; West Nile virus

Indexed keywords

ANTIVIRUS AGENT; FURIN; NONSTRUCTURAL PROTEIN 2; NONSTRUCTURAL PROTEIN 2B; NONSTRUCTURAL PROTEIN 3; PROTEINASE INHIBITOR; RIBAVIRIN; UNCLASSIFIED DRUG; NS2B PROTEIN, FLAVIVIRUS; NS3 PROTEIN, FLAVIVIRUS; RNA HELICASE; SERINE PROTEINASE; VIRAL PROTEIN;

ANTIVIRAL ACTIVITY; ARTICLE; CELL VIABILITY; CONTROLLED STUDY; CRYSTAL STRUCTURE; DENGUE VIRUS; DRUG SYNTHESIS; ENZYME INHIBITION; ENZYME INHIBITOR INTERACTION; ENZYME SPECIFICITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; INHIBITION CONSTANT; NONHUMAN; PLAQUE ASSAY; PRIORITY JOURNAL; VIRUS REPLICATION; WEST NILE VIRUS; ANTAGONISTS AND INHIBITORS; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; DRUG EFFECTS; ENZYMOLOGY; GROWTH, DEVELOPMENT AND AGING; METABOLISM; MICROBIAL SENSITIVITY TEST; STRUCTURE ACTIVITY RELATION; SYNTHESIS;

ANTIVIRAL AGENTS; DENGUE VIRUS; DOSE-RESPONSE RELATIONSHIP, DRUG; FURIN; MICROBIAL SENSITIVITY TESTS; MOLECULAR STRUCTURE; PROTEASE INHIBITORS; RNA HELICASES; SERINE ENDOPEPTIDASES; STRUCTURE-ACTIVITY RELATIONSHIP; VIRAL NONSTRUCTURAL PROTEINS; VIRUS REPLICATION; WEST NILE VIRUS;

EID: 85017315113     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.1080/14756366.2017.1306521     Document Type: Article

References (39)

1. Bhatt S, Gething PW, Brady OJ, et al. The global distribution and burden of dengue. Nature 2013;496:504–7.
2. Suthar MS, Diamond MS, Gale M, Jr. West Nile virus infection and immunity. Nat Rev Microbiol 2013;11:115–28.
3. Thomas SJ, Rothman AL., Trials and tribulations on the path to developing a dengue vaccine. Vaccine 2015;33:D24–31.
4. Hadinegoro SR, Arredondo-Garcia JL, Capeding MR, et al. Efficacy and long-term safety of a dengue vaccine in regions of endemic disease. N Engl J Med 2015;373:1195–206.
5. Villar L, Dayan GH, Arredondo-Garcia JL, et al. Efficacy of a tetravalent dengue vaccine in children in Latin America. N Engl J Med 2015;372:113–23.
6. Vannice KS, Durbin A, Hombach J., Status of vaccine research and development of vaccines for dengue. Vaccine 2016;34:2934–8.
7. Lim SP, Wang QY, Noble CG, et al. Ten years of dengue drug discovery:progress and prospects. Antiviral Res 2013;100:500–19.
8. Lim SP, Shi PY., West Nile virus drug discovery. Viruses 2013;5:2977–3006.
9. Luo D, Vasudevan SG, Lescar J., The flavivirus NS2B-NS3 protease-helicase as a target for antiviral drug development. Antiviral Res 2015;118:148–58.
10. Nitsche C, Holloway S, Schirmeister T, Klein CD., Biochemistry and medicinal chemistry of the dengue virus protease. Chem Rev 2014;114:11348–81.
11. Steuber H, Kanitz M, Ehlert FR, Diederich W., Recent advances in targeting Dengue and West Nile virus proteases using small molecule inhibitors. In:Diederich WE, Steuber H, eds. Therapy of viral infections. Topics in medicinal chemistry. Vol. 15. Berlin, Heidelberg:Springer; 2015:93–141.
12. Chappell KJ, Stoermer MJ, Fairlie DP, Young PR., Insights to substrate binding and processing by West Nile Virus NS3 protease through combined modeling, protease mutagenesis, and kinetic studies. J Biol Chem 2006;281:38448–58.
13. Shiryaev SA, Ratnikov BI, Aleshin AE, et al. Switching the substrate specificity of the two-component NS2B-NS3 flavivirus proteinase by structure-based mutagenesis. J Virol 2007;81:4501–9.
14. Seidah NG, Prat A., The biology and therapeutic targeting of the proprotein convertases. Nat Rev Drug Discov 2012;11:367–83.
15. Lindenbach BD, Murray CL, Thiel H-J, Rice CM., Chapter 25:Flaviviridae. In:David M, Knipe PMH, eds. Fields virology. 6th ed. Philadelphia, PA:Lippincott Williams & Wilkins; 2013:712–46.
16. Shiryaev SA, Ratnikov BI, Chekanov AV, et al. Cleavage targets and the d-arginine-based inhibitors of the West Nile virus NS3 processing proteinase. Biochem J 2006;393:503–11.
17. Lim HA, Joy J, Hill J, San Brian Chia C., Novel agmatine and agmatine-like peptidomimetic inhibitors of the West Nile virus NS2B/NS3 serine protease. Eur J Med Chem 2011;46:3130–4.
18. Lim HA, Ang MJ, Joy J, et al. Novel agmatine dipeptide inhibitors against the West Nile virus NS2B/NS3 protease:a P3 and N-cap optimization study. Eur J Med Chem 2013;62:199–205.
19. Hammamy MZ, Haase C, Hammami M, et al. Development and characterization of new peptidomimetic inhibitors of the West Nile virus NS2B-NS3 protease. ChemMedChem 2013;8:231–41.
20. Weigel LF, Nitsche C, Graf D, et al. Phenylalanine and phenylglycine analogues as arginine mimetics in dengue protease inhibitors. J Med Chem 2015;58:7719–33.
21. Saupe SM, Steinmetzer T., A new strategy for the development of highly potent and selective plasmin inhibitors. J Med Chem 2012;55:1171–80.
22. Bernatowicz MS, Wu Y, Matsueda GR., Urethane protected derivatives of 1-guanylpyrazole for the mild and efficient preparation of guanidines. Tetrahedron Lett 1993;34:3389–92.
23. Elsawy MA, Hewage C, Walker B., Racemisation of N-Fmoc phenylglycine under mild microwave-SPPS and conventional stepwise SPPS conditions:attempts to develop strategies for overcoming this. J Pept Sci 2012;18:302–11.
24. Becker GL, Lu Y, Hardes K, et al. Highly potent inhibitors of proprotein convertase furin as potential drugs for treatment of infectious diseases. J Biol Chem 2012;287:21992–2003.
25. Hardes K, Becker GL, Lu Y, et al. Novel furin inhibitors with potent anti-infectious activity. ChemMedChem 2015;10:1218–31.
26. D’Arcy A, Chaillet M, Schiering N, et al. Purification and crystallization of dengue and West Nile virus NS2B-NS3 complexes. Acta Crystallogr F Struct Biol Cryst Commun 2006;62:157–62.
27. Dixon M., The determination of enzyme inhibitor constants. Biochem J 1953;55:170–1.
28. Nitsche C, Schreier VN, Behnam MA, et al. Thiazolidinone-peptide hybrids as Dengue Virus protease inhibitors with antiviral activity in cell culture. J Med Chem 2013;56:8389–403.
29. Stoermer MJ, Chappell KJ, Liebscher S, et al. Potent cationic inhibitors of West Nile virus NS2B/NS3 protease with serum stability, cell permeability and antiviral activity. J Med Chem 2008;51:5714–21.
30. Heinz FX, Stiasny K., Flaviviruses and their antigenic structure. J Clin Virol 2012;55:289–95.
31. Fuchs SM, Raines RT., Internalization of cationic peptides:the road less (or more?) traveled. Cell Mol Life Sci 2006;63:1819–22.
32. Milletti F., Cell-penetrating peptides:classes, origin, and current landscape. Drug Discov Today 2012;17:850–60.
33. Aleshin AE, Shiryaev SA, Strongin AY, Liddington RC., Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. Protein Sci 2007;16:795–806.
34. Braun PJ, Dennis S, Hofsteenge J, Stone SR., Use of site-directed mutagenesis to investigate the basis for the specificity of hirudin. Biochemistry 1988;27:6517–22.
35. Rydel TJ, Tulinsky A, Bode W, Huber R., Refined structure of the hirudin–thrombin complex. J Mol Biol 1991;221:583–601.
36. Samanta S, Lim TL, Lam Y., Synthesis in vitro evaluation of West Nile virus protease inhibitors based on the 2-{6-[2-(5-phenyl-4H-{1,2,4]triazol-3-ylsulfanyl)acetylamino]benzothiazol-2-ylsul fanyl}acetamide scaffold. ChemMedChem 2013;8:994–1001.
37. Gao Y, Samanta S, Cui T, Lam Y., Synthesis invitro evaluation of West Nile virus protease inhibitors based on the 1,3,4,5-tetrasubstituted 1H-pyrrol-2(5H)-one scaffold. Chem Med Chem 2013;8:1554–60.
38. Wu H, Bock S, Snitko M, et al. Novel Dengue Virus NS2B/NS3 protease inhibitors. Antimicrob Agents Chemother 2015;59:1100–9.
39. Behnam MA, Nitsche C, Boldescu V, Klein CD., The medicinal chemistry of dengue virus. J Med Chem 2016;59:5622–49.