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Volumn 12, Issue 1, 2015, Pages

A small molecule inhibitor of dengue virus type 2 protease inhibits the replication of all four dengue virus serotypes in cell culture

Author keywords

Antiviral therapy; Dengue fever; Dengue protease inhibitor; Dengue virus; NS2b NS3 protease

Indexed keywords

ANTIVIRUS AGENT; BENZIMIDAZOLE DERIVATIVE; PROTEINASE; PROTEINASE INHIBITOR; RECOMBINANT ENZYME; VIRUS ANTIGEN; BENZIMIDAZOLE; NS3 PROTEASE, DENGUE VIRUS; SERINE PROTEINASE;

EID: 84924156322     PISSN: None     EISSN: 1743422X     Source Type: Journal    
DOI: 10.1186/s12985-015-0248-x     Document Type: Article
Times cited : (48)

References (32)
  • 1
    • 84861830178 scopus 로고    scopus 로고
    • The economic burden of dengue
    • Gubler DJ. The economic burden of dengue. Am J Trop Med Hyg. 2012;86:743-4.
    • (2012) Am J Trop Med Hyg. , vol.86 , pp. 743-744
    • Gubler, D.J.1
  • 3
    • 65649125961 scopus 로고    scopus 로고
    • Dengue: Recent advances in biology and current status of translational research
    • Swaminathan S, Khanna N. Dengue: recent advances in biology and current status of translational research. Curr Mol Med. 2009;9:152-73.
    • (2009) Curr Mol Med. , vol.9 , pp. 152-173
    • Swaminathan, S.1    Khanna, N.2
  • 5
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • Knipe DM, Howley PM, editors, 5th ed. Philadelphia: Wolters Kluwer and Lippincott Williams & Wilkins
    • Lindenbach BD, Thiel HJ, Rice CM. Flaviviridae: the viruses and their replication. In: Knipe DM, Howley PM, editors. Field's Virology. 5th ed. Philadelphia: Wolters Kluwer and Lippincott Williams & Wilkins; 2007. p. 1101-52.
    • (2007) Field's Virology , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 9
    • 84908160975 scopus 로고    scopus 로고
    • Clinical efficacy and safety of a novel tetravalent dengue vaccine in healthy children in Asia: A phase 3, randomized, observermasked, placebo-controlled trial
    • Capeding MR, Tran NH, Hadinegoro SRS, Ismail HIHJM, Chotpitayasunondh T, Chua MN, et al. Clinical efficacy and safety of a novel tetravalent dengue vaccine in healthy children in Asia: a phase 3, randomized, observermasked, placebo-controlled trial. Lancet. 2014;384:1358-65.
    • (2014) Lancet. , vol.384 , pp. 1358-1365
    • Capeding, M.R.1    Tran, N.H.2    Hadinegoro, S.R.S.3    Ismail, H.I.H.J.M.4    Chotpitayasunondh, T.5    Chua, M.N.6
  • 10
    • 84868211668 scopus 로고    scopus 로고
    • Protective efficacy of the recombinant, live-attenuated, CYD tetravalent dengue vaccine in Thai schoolchildren: A randomized, controlled phase 2b trial
    • Sabchareon A, Wallace D, Sirivichayakul C, Limkittikul K, Chanthavanich P, Suvannadabba S, et al. Protective efficacy of the recombinant, live-attenuated, CYD tetravalent dengue vaccine in Thai schoolchildren: a randomized, controlled phase 2b trial. Lancet. 2012;380:1559-67.
    • (2012) Lancet. , vol.380 , pp. 1559-1567
    • Sabchareon, A.1    Wallace, D.2    Sirivichayakul, C.3    Limkittikul, K.4    Chanthavanich, P.5    Suvannadabba, S.6
  • 14
    • 0036569001 scopus 로고    scopus 로고
    • Differing influences of virus burden and immune activation on disease severity in secondary dengue-3 virus infections
    • Libraty DH, Endy TP, Houng HSH, Greene S, Kalyanarooj S, Suntayakorn S, et al. Differing influences of virus burden and immune activation on disease severity in secondary dengue-3 virus infections. J Infect Dis. 2002;185:1213-21.
    • (2002) J Infect Dis. , vol.185 , pp. 1213-1221
    • Libraty, D.H.1    Endy, T.P.2    Houng, H.S.H.3    Greene, S.4    Kalyanarooj, S.5    Suntayakorn, S.6
  • 16
    • 53249121029 scopus 로고    scopus 로고
    • Towards the design of antiviral inhibitors against flaviviruses: The case for the multifunctional NS3 protein from dengue virus as a target
    • Lescar J, Luo D, Xu T, Sampath A, Lim SP, Canard B, et al. 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.
    • (2008) Antiviral Res. , vol.80 , pp. 94-101
    • Lescar, J.1    Luo, D.2    Xu, T.3    Sampath, A.4    Lim, S.P.5    Canard, B.6
  • 17
    • 0027499688 scopus 로고
    • Deletion analysis of dengue virus type 4 nonstructural protein NS2b: Identification of a domain required for NS2b-NS3 protease activity
    • Falgout B, Miller RH, Lai CJ. Deletion analysis of dengue virus type 4 nonstructural protein NS2b: identification of a domain required for NS2b-NS3 protease activity. J Virol. 1993;67:2034-42.
    • (1993) J Virol. , vol.67 , pp. 2034-2042
    • Falgout, B.1    Miller, R.H.2    Lai, C.J.3
  • 18
    • 0025201350 scopus 로고
    • Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavage in the viral polyprotein
    • Chambers TJ, Weir RC, Grakoui A, McCourt DW, Bazan JF, Fletterick RJ, et al. Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavage in the viral polyprotein. Proc Natl Acad Sci USA. 1990;87:8898-902.
    • (1990) Proc Natl Acad Sci USA. , vol.87 , pp. 8898-8902
    • Chambers, T.J.1    Weir, R.C.2    Grakoui, A.3    McCourt, D.W.4    Bazan, J.F.5    Fletterick, R.J.6
  • 19
    • 0027486484 scopus 로고
    • Mutagenesis of the yellow fever virus NS2b protein: Effects on proteolytic processing, NS2b-NS3 complex formation, and viral replication
    • Chambers TJ, Nestorowicz A, Amberg SM, Rice CM. Mutagenesis of the yellow fever virus NS2b protein: effects on proteolytic processing, NS2b-NS3 complex formation, and viral replication. J Virol. 1993;67:6797-807.
    • (1993) J Virol. , vol.67 , pp. 6797-6807
    • Chambers, T.J.1    Nestorowicz, A.2    Amberg, S.M.3    Rice, C.M.4
  • 20
    • 23344446921 scopus 로고    scopus 로고
    • Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries
    • Li J, Lim SP, Beer D, Patel V, Wen D, Tumanut C, et al. Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries. J Biol Chem. 2005;280:28766-74.
    • (2005) J Biol Chem. , vol.280 , pp. 28766-28774
    • Li, J.1    Lim, S.P.2    Beer, D.3    Patel, V.4    Wen, D.5    Tumanut, C.6
  • 21
    • 0035824539 scopus 로고    scopus 로고
    • Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2b co-factor, small peptide substrates, and inhibitors
    • Leung D, Schroder K, White H, Fang NX, Stoermer MJ, Abbenante G, et al. 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;276:45762-71.
    • (2001) J Biol Chem. , vol.276 , pp. 45762-45771
    • Leung, D.1    Schroder, K.2    White, H.3    Fang, N.X.4    Stoermer, M.J.5    Abbenante, G.6
  • 22
    • 0034616194 scopus 로고    scopus 로고
    • Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro
    • Yusof R, Clum S, Wetzel M, Murthy HMK, 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;275:9963-9.
    • (2000) J Biol Chem. , vol.275 , pp. 9963-9969
    • Yusof, R.1    Clum, S.2    Wetzel, M.3    Murthy, H.M.K.4    Padmanabhan, R.5
  • 23
    • 84873723914 scopus 로고    scopus 로고
    • Discovery of novel inhibitors targeting the Mycobacterium tuberculosis O-acetylserine sulfhydrylase (CysK1) using virtual high-throughput screening
    • Jean Kumar VU, Poyraz O, Saxena S, Schnell R, Yogeeswari P, Schneider G, et al. Discovery of novel inhibitors targeting the Mycobacterium tuberculosis O-acetylserine sulfhydrylase (CysK1) using virtual high-throughput screening. Biorg Med Chem Lett. 2013;23:1182-6.
    • (2013) Biorg Med Chem Lett. , vol.23 , pp. 1182-1186
    • Jean Kumar, V.U.1    Poyraz, O.2    Saxena, S.3    Schnell, R.4    Yogeeswari, P.5    Schneider, G.6
  • 24
    • 84883167771 scopus 로고    scopus 로고
    • Structure-guided design of novel thiazolidine inhibitors of O-acetyl serine sulfhydrylase from Mycobacterium tuberculosis
    • Poyraz O, Jeankumar VU, Saxena S, Schnell R, Haraldsson M, Yogeeswari P, et al. Structure-guided design of novel thiazolidine inhibitors of O-acetyl serine sulfhydrylase from Mycobacterium tuberculosis. J Med Chem. 2013;56:6457-66.
    • (2013) J Med Chem. , vol.56 , pp. 6457-6466
    • Poyraz, O.1    Jeankumar, V.U.2    Saxena, S.3    Schnell, R.4    Haraldsson, M.5    Yogeeswari, P.6
  • 25
    • 84904284634 scopus 로고    scopus 로고
    • Allosteric pocket of the dengue virus (serotype 2) NS2B/NS3 protease: In silico ligand screening and molecular dynamics studies of inhibition
    • Mukhametov A, Newhouse EI, Aziz NA, Saito JA, Alam M. Allosteric pocket of the dengue virus (serotype 2) NS2B/NS3 protease: In silico ligand screening and molecular dynamics studies of inhibition. J Mol Graph Model. 2014;52:103-13.
    • (2014) J Mol Graph Model. , vol.52 , pp. 103-113
    • Mukhametov, A.1    Newhouse, E.I.2    Aziz, N.A.3    Saito, J.A.4    Alam, M.5
  • 26
    • 52049104700 scopus 로고    scopus 로고
    • Docking of noncompetitive inhibitors into dengue virus type 2 protease: Understanding the interactions with allosteric binding sites
    • Othman R, Kiat TS, Khalid N, Yusof R, Newhouse EI, Newhouse JS, et al. Docking of noncompetitive inhibitors into dengue virus type 2 protease: understanding the interactions with allosteric binding sites. J Chem Inf Model. 2008;48:1582-91.
    • (2008) J Chem Inf Model. , vol.48 , pp. 1582-1591
    • Othman, R.1    Kiat, T.S.2    Khalid, N.3    Yusof, R.4    Newhouse, E.I.5    Newhouse, J.S.6
  • 27
    • 84864605865 scopus 로고    scopus 로고
    • Adenovirus-delivered short hairpin RNA targeting a conserved site in the 5' non-translated region inhibits all four serotypes of dengue viruses
    • Korrapati AB, Swaminathan G, Singh A, Khanna N, Swaminathan S. Adenovirus-delivered short hairpin RNA targeting a conserved site in the 5' non-translated region inhibits all four serotypes of dengue viruses. PLoS Negl Trop Dis. 2012;6:e1735.
    • (2012) PLoS Negl Trop Dis. , vol.6 , pp. e1735
    • Korrapati, A.B.1    Swaminathan, G.2    Singh, A.3    Khanna, N.4    Swaminathan, S.5
  • 28
    • 44049104986 scopus 로고    scopus 로고
    • Use of a commercial enzyme immunoassay to monitor dengue virus replication in cultured cells
    • Ludert JE, Mosso C, Ceballos-Olvera I, Del Angel RM. Use of a commercial enzyme immunoassay to monitor dengue virus replication in cultured cells. Virol J. 2008;5:51.
    • (2008) Virol J. , vol.5 , pp. 51
    • Ludert, J.E.1    Mosso, C.2    Ceballos-Olvera, I.3    Del Angel, R.M.4
  • 29
    • 33847042742 scopus 로고    scopus 로고
    • A dengue fever viremia model in mice shows reduction in viral replication and suppression of the inflammatory response after treatment with antiviral drugs
    • Schul W, Liu W, Xu HY, Flamand M, Vasudevan SG. A dengue fever viremia model in mice shows reduction in viral replication and suppression of the inflammatory response after treatment with antiviral drugs. J Infect Dis. 2007;195:665-74.
    • (2007) J Infect Dis. , vol.195 , pp. 665-674
    • Schul, W.1    Liu, W.2    Xu, H.Y.3    Flamand, M.4    Vasudevan, S.G.5
  • 30
  • 31
    • 77958100661 scopus 로고    scopus 로고
    • Dengue virus non-structural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis
    • Heaton NS, Perera R, Berger KL, Khadka S, La Count DJ, Kuhn RJ, et al. Dengue virus non-structural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis. Proc Natl Acad Sci USA. 2010;107:17345-50.
    • (2010) Proc Natl Acad Sci USA. , vol.107 , pp. 17345-17350
    • Heaton, N.S.1    Perera, R.2    Berger, K.L.3    Khadka, S.4    La Count, D.J.5    Kuhn, R.J.6
  • 32
    • 12144289984 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring.1. Method and assessment of docking accuracy
    • Friesner RA, Banks JL, Murphy RB, Halgren TA, Klicic JJ, Mainz DT, et al. Glide: a new approach for rapid, accurate docking and scoring.1. Method and assessment of docking accuracy. J Med Chem. 2004;47:1739-49.
    • (2004) J Med Chem. , vol.47 , pp. 1739-1749
    • Friesner, R.A.1    Banks, J.L.2    Murphy, R.B.3    Halgren, T.A.4    Klicic, J.J.5    Mainz, D.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.