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Volumn 4, Issue 11, 2010, Pages

High affinity human antibody fragments to dengue virus non-structural protein 3

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HELICASE; NONSTRUCTURAL PROTEIN 2B; NONSTRUCTURAL PROTEIN 3; UNCLASSIFIED DRUG; IMMUNOGLOBULIN F(AB) FRAGMENT; NS3 PROTEIN, FLAVIVIRUS; RNA HELICASE; SERINE PROTEINASE; VIRUS ANTIBODY; VIRUS PROTEIN;

EID: 78649783890     PISSN: None     EISSN: None     Source Type: Journal    
DOI: 10.1371/journal.pntd.0000881     Document Type: Article
Times cited : (34)

References (32)
  • 1
    • 0031823546 scopus 로고    scopus 로고
    • Dengue and dengue hemorrhagic fever
    • Gubler DJ (1998) Dengue and dengue hemorrhagic fever. Clin Microbiol Rev 11: 480-496.
    • (1998) Clin Microbiol Rev , vol.11 , pp. 480-496
    • Gubler, D.J.1
  • 2
    • 0024341494 scopus 로고
    • N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases
    • Gorbalenya AE, Donchenko AP, Koonin EV, Blinov VM (1989) N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases. Nucleic Acids Res 17: 3889-3897.
    • (1989) Nucleic Acids Res , vol.17 , pp. 3889-3897
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Koonin, E.V.3    Blinov, V.M.4
  • 3
    • 0027285404 scopus 로고
    • Dengue 2 virus NS2B and NS3 form a stable complex that can cleave NS3 within the helicase domain
    • Arias CF, Preugschat F, Strauss JH (1993) Dengue 2 virus NS2B and NS3 form a stable complex that can cleave NS3 within the helicase domain. Virology 193: 888-899.
    • (1993) Virology , vol.193 , pp. 888-899
    • Arias, C.F.1    Preugschat, F.2    Strauss, J.H.3
  • 4
    • 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 HM, Padmanabhan R (2000) 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 275: 9963-9969.
    • (2000) J Biol Chem , vol.275 , pp. 9963-9969
    • Yusof, R.1    Clum, S.2    Wetzel, M.3    Murthy, H.M.4    Padmanabhan, R.5
  • 5
    • 0035824539 scopus 로고    scopus 로고
    • Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B cofactor, small peptide substrates, and inhibitors
    • Leung D, Schroder K, White H, Fang NX, Stoermer MJ, et al. (2001) Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B cofactor, small peptide substrates, and inhibitors. J Biol Chem 276: 45762-45771.
    • (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
  • 6
    • 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, et al. (2005) Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries. J Biol Chem 280: 28766-28774.
    • (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
  • 7
    • 23244464646 scopus 로고    scopus 로고
    • Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A
    • Xu T, Sampath A, Chao A, Wen D, Nanao M, et al. (2005) Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A. Journal of Virology 79: 10278-10288.
    • (2005) Journal of Virology , vol.79 , pp. 10278-10288
    • Xu, T.1    Sampath, A.2    Chao, A.3    Wen, D.4    Nanao, M.5
  • 8
    • 37349023165 scopus 로고    scopus 로고
    • Crystal structure of the NS3 protease-helicase from dengue virus
    • Luo D, Xu T, Hunke C, Grüber G, Vasudevan SG, et al. (2008) Crystal structure of the NS3 protease-helicase from dengue virus. Journal of Virology 82: 173-183.
    • (2008) Journal of Virology , vol.82 , pp. 173-183
    • Luo, D.1    Xu, T.2    Hunke, C.3    Grüber, G.4    Vasudevan, S.G.5
  • 9
    • 72849147739 scopus 로고    scopus 로고
    • Crystal structure of a novel conformational state of the flavivirus NS3 protein: Implications for polyprotein processing and viral replication
    • Assenberg R, Mastrangelo E, Walter TS, Verma A, Milani M, et al. (2009) Crystal structure of a novel conformational state of the flavivirus NS3 protein: implications for polyprotein processing and viral replication. Journal of Virology 83: 12895-12906.
    • (2009) Journal of Virology , vol.83 , pp. 12895-12906
    • Assenberg, R.1    Mastrangelo, E.2    Walter, T.S.3    Verma, A.4    Milani, M.5
  • 10
    • 33751254102 scopus 로고    scopus 로고
    • Recent advances in deciphering viral and host determinants of dengue virus replication and pathogenesis
    • Clyde K, Kyle JL, Harris E (2006) Recent advances in deciphering viral and host determinants of dengue virus replication and pathogenesis. Journal of Virology 80: 11418-11431.
    • (2006) Journal of Virology , vol.80 , pp. 11418-11431
    • Clyde, K.1    Kyle, J.L.2    Harris, E.3
  • 12
    • 62949093951 scopus 로고    scopus 로고
    • Tropism of dengue virus in mice and humans defined by viral nonstructural protein 3-specific immunostaining
    • Balsitis SJ, Coloma J, Castro G, Alava A, Flores D, et al. (2009) Tropism of dengue virus in mice and humans defined by viral nonstructural protein 3-specific immunostaining. Am J Trop Med Hyg 80: 416-424.
    • (2009) Am J Trop Med Hyg , vol.80 , pp. 416-424
    • Balsitis, S.J.1    Coloma, J.2    Castro, G.3    Alava, A.4    Flores, D.5
  • 13
    • 58149116426 scopus 로고    scopus 로고
    • Production of a monoclonal antibody against non-structural protein 3 of dengue-2 virus by intrasplenic injection
    • Chen Z, Tian Y, Liu L, An J (2008) Production of a monoclonal antibody against non-structural protein 3 of dengue-2 virus by intrasplenic injection. Hybridoma (Larchmt) 27: 467-471.
    • (2008) Hybridoma (Larchmt) , vol.27 , pp. 467-471
    • Chen, Z.1    Tian, Y.2    Liu, L.3    An, J.4
  • 15
    • 0025308282 scopus 로고
    • Passive protection studies in mice with monoclonal antibodies directed against the non-structural protein NS3 of dengue 1 virus
    • Tan CH, Yap EH, Singh M, Deubel V, Chan YC (1990) Passive protection studies in mice with monoclonal antibodies directed against the non-structural protein NS3 of dengue 1 virus. J Gen Virol 71(Pt 3): 745-749.
    • (1990) J Gen Virol , vol.71 , Issue.Pt 3 , pp. 745-749
    • Tan, C.H.1    Yap, E.H.2    Singh, M.3    Deubel, V.4    Chan, Y.C.5
  • 16
    • 0025838021 scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces: The gene III site
    • Barbas CF, Kang AS, Lerner RA, Benkovic SJ (1991) Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc Natl Acad Sci USA 88: 7978-7982.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7978-7982
    • Barbas, C.F.1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4
  • 17
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom HR, Griffiths AD, Johnson KS, Chiswell DJ, Hudson P, et al. (1991) Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res 19: 4133-4137.
    • (1991) Nucleic Acids Res , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5
  • 18
    • 57149091105 scopus 로고    scopus 로고
    • Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein
    • Luo D, Xu T, Watson RP, Scherer-Becker D, Sampath A, et al. (2008) Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein. EMBO J 27: 3209-3219.
    • (2008) EMBO J , vol.27 , pp. 3209-3219
    • Luo, D.1    Xu, T.2    Watson, R.P.3    Scherer-Becker, D.4    Sampath, A.5
  • 19
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41: 207-234.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 20
    • 0033603596 scopus 로고    scopus 로고
    • A large non-immunized human Fab fragment phage library that permits rapid isolation and kinetic analysis of high affinity antibodies
    • de Haard HJ, van Neer N, Reurs A, Hufton SE, Roovers RC, et al. (1999) A large non-immunized human Fab fragment phage library that permits rapid isolation and kinetic analysis of high affinity antibodies. J Biol Chem 274: 18218-18230.
    • (1999) J Biol Chem , vol.274 , pp. 18218-18230
    • de Haard, H.J.1    van Neer, N.2    Reurs, A.3    Hufton, S.E.4    Roovers, R.C.5
  • 21
    • 56049097199 scopus 로고    scopus 로고
    • Neutralizing human monoclonal antibody against H5N1 influenza HA selected from a Fab-phage display library
    • Lim APC, Chan CEZ, Wong SKK, Chan AHY, Ooi EE, et al. (2008) Neutralizing human monoclonal antibody against H5N1 influenza HA selected from a Fab-phage display library. Virol J 5: 130.
    • (2008) Virol J , vol.5 , pp. 130
    • Lim, A.P.C.1    Chan, C.E.Z.2    Wong, S.K.K.3    Chan, A.H.Y.4    Ooi, E.E.5
  • 22
    • 47749152947 scopus 로고    scopus 로고
    • The two-component NS2B-NS3 proteinase represses DNA unwinding activity of the West Nile virus NS3 helicase
    • Chernov AV, Shiryaev SA, Aleshin AE, Ratnikov BI, Smith JW, et al. (2008) The two-component NS2B-NS3 proteinase represses DNA unwinding activity of the West Nile virus NS3 helicase. J Biol Chem 283: 17270-17278.
    • (2008) J Biol Chem , vol.283 , pp. 17270-17278
    • Chernov, A.V.1    Shiryaev, S.A.2    Aleshin, A.E.3    Ratnikov, B.I.4    Smith, J.W.5
  • 23
    • 65549085229 scopus 로고    scopus 로고
    • On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes
    • Rajamanonmani R, Nkenfou C, Clancy P, Yau YH, Shochat SG, et al. (2009) On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes. J Gen Virol 90: 799-809.
    • (2009) J Gen Virol , vol.90 , pp. 799-809
    • Rajamanonmani, R.1    Nkenfou, C.2    Clancy, P.3    Yau, Y.H.4    Shochat, S.G.5
  • 24
    • 0033711628 scopus 로고    scopus 로고
    • Diversity in the CDR3 Region of VH Is Sufficient for Most Antibody Specificities
    • Xu JL, Davis MM (2000) Diversity in the CDR3 Region of VH Is Sufficient for Most Antibody Specificities. Immunity 13: 37-45.
    • (2000) Immunity , vol.13 , pp. 37-45
    • Xu, J.L.1    Davis, M.M.2
  • 25
    • 11044235782 scopus 로고    scopus 로고
    • The nature of target-unrelated peptides recovered in the screening of phage-displayed random peptide libraries with antibodies
    • Menendez A, Scott JK (2005) The nature of target-unrelated peptides recovered in the screening of phage-displayed random peptide libraries with antibodies. Anal Biochem 336: 145-157.
    • (2005) Anal Biochem , vol.336 , pp. 145-157
    • Menendez, A.1    Scott, J.K.2
  • 26
    • 77951237083 scopus 로고    scopus 로고
    • Isolation and characterization of selective and potent human Fab inhibitors directed to the active site region of the two-component NS2B-NS3 proteinase of West Nile virus
    • Shiryaev SA, Radichev IA, Ratnikov BI, Aleshin AE, Gawlik K, et al. (2010) Isolation and characterization of selective and potent human Fab inhibitors directed to the active site region of the two-component NS2B-NS3 proteinase of West Nile virus. Biochem J 427: 369-376.
    • (2010) Biochem J , vol.427 , pp. 369-376
    • Shiryaev, S.A.1    Radichev, I.A.2    Ratnikov, B.I.3    Aleshin, A.E.4    Gawlik, K.5
  • 27
    • 5344260388 scopus 로고    scopus 로고
    • The RNA helicase, nucleotide 59-triphosphatase, and RNA 59-triphosphatase activities of Dengue virus protein NS3 are Mg2+-dependent and require a functional Walker B motif in the helicase catalytic core
    • Benarroch D, Selisko B, Locatelli GA, Maga G, Romette J-L, et al. (2004) The RNA helicase, nucleotide 59-triphosphatase, and RNA 59-triphosphatase activities of Dengue virus protein NS3 are Mg2+-dependent and require a functional Walker B motif in the helicase catalytic core. Virology 328: 208-218.
    • (2004) Virology , vol.328 , pp. 208-218
    • Benarroch, D.1    Selisko, B.2    Locatelli, G.A.3    Maga, G.4    Romette, J.-L.5
  • 28
    • 0032976077 scopus 로고    scopus 로고
    • The serine protease and RNA-stimulated nucleoside triphosphatase and RNA helicase functional domains of dengue virus type 2 NS3 converge within a region of 20 amino acids
    • Li H, Clum S, You S, Ebner KE, Padmanabhan R (1999) The serine protease and RNA-stimulated nucleoside triphosphatase and RNA helicase functional domains of dengue virus type 2 NS3 converge within a region of 20 amino acids. Journal of Virology 73: 3108-3116.
    • (1999) Journal of Virology , vol.73 , pp. 3108-3116
    • Li, H.1    Clum, S.2    You, S.3    Ebner, K.E.4    Padmanabhan, R.5
  • 29
    • 0037184036 scopus 로고    scopus 로고
    • The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin beta 1 and importin alpha/betarecognized nuclear localization signals
    • Brooks AJ, Johansson M, John AV, Xu Y, Jans DA, et al. (2002) The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin beta 1 and importin alpha/betarecognized nuclear localization signals. J Biol Chem 277: 36399-36407.
    • (2002) J Biol Chem , vol.277 , pp. 36399-36407
    • Brooks, A.J.1    Johansson, M.2    John, A.V.3    Xu, Y.4    Jans, D.A.5
  • 30
    • 77953306294 scopus 로고    scopus 로고
    • Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications
    • Luo D, Wei N, Doan DN, Paradkar PN, Chong Y, et al. (2010) Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications. J Biol Chem 285: 18817-188127.
    • (2010) J Biol Chem , vol.285 , pp. 18817-188127
    • Luo, D.1    Wei, N.2    Doan, D.N.3    Paradkar, P.N.4    Chong, Y.5
  • 31
    • 77957296223 scopus 로고    scopus 로고
    • Fine-tuning DNA/albumin polyelectrolyte interactions to produce the efficient transfection agent cBSA-147
    • Sep 2. [Epub ahead of print]
    • Eisele K, Gropeanu RA, Zehendner CM, Rouhanipour A, Ramanathan A, et al. (2010) Fine-tuning DNA/albumin polyelectrolyte interactions to produce the efficient transfection agent cBSA-147. Biomaterials, Sep 2. [Epub ahead of print].
    • (2010) Biomaterials
    • Eisele, K.1    Gropeanu, R.A.2    Zehendner, C.M.3    Rouhanipour, A.4    Ramanathan, A.5
  • 32
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


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