A small compound targeting the interaction between nonstructural proteins 2B and 3 inhibits dengue virus replication

Biochemical and Biophysical Research Communications

Volumn 440, Issue 3, 2013, Pages 393-398

  Pambudi, Sabar ^a   Kawashita, Norihito ^a,b   Phanthanawiboon, Supranee ^a   Omokoko, Magot Diata ^a   Masrinoul, Promsin ^a   Yamashita, Akifumi ^a   Limkittikul, Kriengsak ^c   Yasunaga, Teruo ^a   Takagi, Tatsuya ^b   Ikuta, Kazuyoshi ^a   Kurosu, Takeshi ^a  

^a OSAKA UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c MAHIDOL UNIVERSITY   (Thailand)

Author keywords

Antiviral; Dengue virus; Infectious diseases; NS2B NS3 protease; Re emerging infection

Indexed keywords

NONSTRUCTURAL PROTEIN NS2B; NONSTRUCTURAL PROTEIN NS3; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ARTICLE; BINDING SITE; DENGUE VIRUS; DENGUE VIRUS 1; DENGUE VIRUS 2; DENGUE VIRUS 3; DENGUE VIRUS 4; ENZYME KINETICS; JAPANESE ENCEPHALITIS VIRUS; MOLECULAR DOCKING; MOLECULAR LIBRARY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TARGETING; REFERENCE DATABASE; SEROTYPE; STEADY STATE; VIRUS INHIBITION; VIRUS REPLICATION;

DENGUE VIRUS; JAPANESE ENCEPHALITIS VIRUS;

ANTIVIRAL; DENGUE VIRUS; INFECTIOUS DISEASES; NS2B/NS3 PROTEASE; RE-EMERGING INFECTION;

ANTIVIRAL AGENTS; COMPUTER SIMULATION; DENGUE; HUMANS; MODELS, CHEMICAL; NAPHTHOLS; PROTEIN CONFORMATION; SERINE PROTEASES; SMALL MOLECULE LIBRARIES; SULFONAMIDES; VIRAL NONSTRUCTURAL PROTEINS; VIRUS REPLICATION;

EID: 84888127965     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.09.078     Document Type: Article

References (23)

1. World Health Organization, Dengue and severe dengue Fact sheet N°117, 2012. .
2. Lindenbach D.S., Rice C.M. Flaviviruses: the viruses and their replication. Fields Virology 2001, 991-1042. Lippincott-Raven, Philadelphia. fourth ed. B.N. Fields, D.M. Knipe, P.M. Howley (Eds.).
3. Falgout B., Pethel M., Zhang Y.M., Lai C.J. Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins. J. Virol. 1991, 65:2467-2475.
4. Zhang L., Mohan P.M., Padmanabhan R. Processing and localization of dengue virus type 2 polyprotein precursor NS3-NS4A-NS4B-NS5. J. Virol. 1992, 66:7549-7554.
5. Cahour A., Falgout B., Lai C.J. Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease. J. Virol. 1992, 66:1535-1542.
6. Chambers T.J., Nestorowicz A., Amberg S.M., Rice C.M. Mutagenesis of the yellow fever virus NS2B protein: effects on proteolytic processing, NS2B-NS3 complex formation, and viral replication. J. Virol. 1993, 67:6797-6807.
7. Leung D., Schroder K., White H., Fang N.X., Stoermer M.J., Abbenante G., Martin J.L., Young P.R., Fairlie D.P. Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors. J. Biol. Chem. 2001, 276:45762-45771.
8. Melino S., Fucito S., Campagna A., Wrubl F., Gamarnik A., Cicero D.O., Paci M. The active essential CFNS3d protein complex. FEBS J. 2006, 273:3650-3662.
9. Clum S., Ebner K.E., Padmanabhan R. Cotranslational membrane insertion of the serine proteinase precursor NS2B-NS3 (Pro) of dengue virus type 2 is required for efficient in vitro processing and is mediated through the hydrophobic regions of NS2B. J. Biol. Chem. 1997, 272:30715-30723.
10. de la Cruz L., Nguyen T.H., Ozawa K., Shin J., Graham B., Huber T., Otting G. Binding of low molecular weight inhibitors promotes large conformational changes in the dengue virus NS2B-NS3 protease: fold analysis by pseudocontact shifts. J. Am. Chem. Soc. 2011, 133:19205-19215.
11. Noble C.G., Seh C.C., Chao A.T., Shi P.Y. Ligand-bound structures of the dengue virus protease reveal the active conformation. J. Virol. 2012, 86:438-446.
12. Lescar J., Luo D., Xu T., Sampath A., Lim S.P., Canard B., Vasudevan S.G. Towards the design of antiviral inhibitors against flaviviruses: the case for the multifunctional NS3 protein from dengue virus as a target. Antiviral Res. 2008, 80:94-101.
13. Kurosu T., Khamlert C., Phanthanawiboon S., Ikuta K., Anantapreecha S. Highly efficient rescue of dengue virus using a co-culture system with mosquito/mammalian cells. Biochem. Biophys. Res. Commun. 2010, 394:398-404.
14. Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 1983, 65:55-63.
15. Yusof R., Clum S., Wetzel M., Murthy H.M., Padmanabhan R. Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro. J. Biol. Chem. 2000, 275:9963-9969.
16. Mueller N.H., Yon C., Ganesh V.K., Padmanabhan R. Characterization of the West Nile virus protease substrate specificity and inhibitors. Int. J. Biochem. Cell Biol. 2007, 39:606-614.
17. Erbel P., Schiering N., D'Arcy A., Renatus M., Kroemer M., Lim S.P., Yin Z., Keller T.H., Vasudevan S.G., Hommel U. Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus. Nat. Struct. Mol. Biol. 2006, 13:372-373.
18. Tomlinson S.M., Malmstrom R.D., Russo A., Mueller N., Pang Y.P., Watowich S.J. Structure-based discovery of dengue virus protease inhibitors. Antiviral Res. 2009, 82:110-114.
19. Asselah T., Marcellin P. New direct-acting antivirals' combination for the treatment of chronic hepatitis C. Liver Int. 2011, 31(Suppl. 1):68-77.
20. Naggie S., Patel K., McHutchison J. Hepatitis C virus directly acting antivirals: current developments with NS3/4A HCV serine protease inhibitors. J. Antimicrob. Chemother. 2010, 65:2063-2069.
21. Wensing A.M., van Maarseveen N.M., Nijhuis M. Fifteen years of HIV protease inhibitors: raising the barrier to resistance. Antiviral Res. 2010, 85:59-74.
22. Erbel P., D'Arcy A., Schiering N., Renatus M., Kroemer M., Lim S.P., Yin Z., Keller T.H., Vasudevan S.G., Hommel U. Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus. Nat. Struct. Mol. Biol. 2006, 13:372-373.
23. Phong W.Y., Moreland N.J., Lim S.P., Wen D., Paradkar P.N., Vasudevan S.G. Dengue protease activity: the structural integrity and interaction of NS2B with NS3 protease and its potential as a drug target. Biosci. Rep. 2011, 31:399-409.