Modulation of the Nucleoside Triphosphatase/RNA Helicase and 5′-RNA Triphosphatase Activities of Dengue Virus Type 2 Nonstructural Protein 3 (NS3) by Interaction with NS5, the RNA-dependent RNA Polymerase
Dengue virus type 2 (DEN2), a member of the Flaviviridae family, is a re-emerging human pathogen of global significance. DEN2 nonstructural protein 3 (NS3) has a serine protease domain (NS3-pro) and requires the hydrophilic domain of NS2B (NS2BH) for activation. NS3 is also an RNA-stimulated nucleos...
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Published in | The Journal of biological chemistry Vol. 280; no. 29; pp. 27412 - 27419 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier Inc
22.07.2005
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Abstract | Dengue virus type 2 (DEN2), a member of the Flaviviridae family, is a re-emerging human pathogen of global significance. DEN2 nonstructural protein 3 (NS3) has a serine protease domain (NS3-pro) and requires the hydrophilic domain of NS2B (NS2BH) for activation. NS3 is also an RNA-stimulated nucleoside triphosphatase (NTPase)/RNA helicase and a 5′-RNA triphosphatase (RTPase). In this study the first biochemical and kinetic properties of full-length NS3 (NS3FL)-associated NTPase, RTPase, and RNA helicase are presented. The NS3FL showed an enhanced RNA helicase activity compared with the NS3-pro-minus NS3, which was further enhanced by the presence of the NS2BH (NS2BH-NS3FL). An active protease catalytic triad is not required for the stimulatory effect, suggesting that the overall folding of the N-terminal protease domain contributes to this enhancement. In DEN2-infected mammalian cells, NS3 and NS5, the viral 5′-RNA methyltransferase/polymerase, exist as a complex. Therefore, the effect of NS5 on the NS3 NTPase activity was examined. The results show that NS5 stimulated the NS3 NTPase and RTPase activities. The NS5 stimulation of NS3 NTPase was dose-dependent until an equimolar ratio was reached. Moreover, the conserved motif, 184RKRK, of NS3 played a crucial role in binding to RNA substrate and modulating the NTPase/RNA helicase and RTPase activities of NS3. |
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AbstractList | Dengue virus type 2 (DEN2), a member of the Flaviviridae family, is a re-emerging human pathogen of global significance. DEN2 nonstructural protein 3 (NS3) has a serine protease domain (NS3-pro) and requires the hydrophilic domain of NS2B (NS2BH) for activation. NS3 is also an RNA-stimulated nucleoside triphosphatase (NTPase)/RNA helicase and a 5′-RNA triphosphatase (RTPase). In this study the first biochemical and kinetic properties of full-length NS3 (NS3FL)-associated NTPase, RTPase, and RNA helicase are presented. The NS3FL showed an enhanced RNA helicase activity compared with the NS3-pro-minus NS3, which was further enhanced by the presence of the NS2BH (NS2BH-NS3FL). An active protease catalytic triad is not required for the stimulatory effect, suggesting that the overall folding of the N-terminal protease domain contributes to this enhancement. In DEN2-infected mammalian cells, NS3 and NS5, the viral 5′-RNA methyltransferase/polymerase, exist as a complex. Therefore, the effect of NS5 on the NS3 NTPase activity was examined. The results show that NS5 stimulated the NS3 NTPase and RTPase activities. The NS5 stimulation of NS3 NTPase was dose-dependent until an equimolar ratio was reached. Moreover, the conserved motif, 184RKRK, of NS3 played a crucial role in binding to RNA substrate and modulating the NTPase/RNA helicase and RTPase activities of NS3. Dengue virus type 2 (DEN2), a member of the Flaviviridae family, is a re-emerging human pathogen of global significance. DEN2 nonstructural protein 3 (NS3) has a serine protease domain (NS3-pro) and requires the hydrophilic domain of NS2B (NS2BH) for activation. NS3 is also an RNA-stimulated nucleoside triphosphatase (NTPase)/RNA helicase and a 5'-RNA triphosphatase (RTPase). In this study the first biochemical and kinetic properties of full-length NS3 (NS3 sub(FL))-associated NTPase, RTPase, and RNA helicase are presented. The NS3 sub(FL) showed an enhanced RNA helicase activity compared with the NS3-pro-minus NS3, which was further enhanced by the presence of the NS2BH (NS2BH-NS3 sub(FL)). An active protease catalytic triad is not required for the stimulatory effect, suggesting that the overall folding of the N-terminal protease domain contributes to this enhancement. In DEN2-infected mammalian cells, NS3 and NS5, the viral 5'-RNA methyltransferase/polymerase, exist as a complex. Therefore, the effect of NS5 on the NS3 NTPase activity was examined. The results show that NS5 stimulated the NS3 NTPase and RTPase activities. The NS5 stimulation of NS3 NTPase was dose-dependent until an equimolar ratio was reached. Moreover, the conserved motif, super(184)RKRK, of NS3 played a crucial role in binding to RNA substrate and modulating the NTPase/RNA helicase and RTPase activities of NS3. |
Author | Teramoto, Tadahisa Yon, Changsuek Phelan, Jessica Mueller, Niklaus Murthy, Krishna H.M. Padmanabhan, R. Ganesh, Vannakambadi K. |
Author_xml | – sequence: 1 givenname: Changsuek surname: Yon fullname: Yon, Changsuek organization: Department of Microbiology and Immunology, Georgetown University School of Medicine, Washington D. C. 20057 and – sequence: 2 givenname: Tadahisa surname: Teramoto fullname: Teramoto, Tadahisa organization: Department of Microbiology and Immunology, Georgetown University School of Medicine, Washington D. C. 20057 and – sequence: 3 givenname: Niklaus surname: Mueller fullname: Mueller, Niklaus organization: Department of Microbiology and Immunology, Georgetown University School of Medicine, Washington D. C. 20057 and – sequence: 4 givenname: Jessica surname: Phelan fullname: Phelan, Jessica organization: Department of Microbiology and Immunology, Georgetown University School of Medicine, Washington D. C. 20057 and – sequence: 5 givenname: Vannakambadi K. surname: Ganesh fullname: Ganesh, Vannakambadi K. organization: Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, Alabama 35294 – sequence: 6 givenname: Krishna H.M. surname: Murthy fullname: Murthy, Krishna H.M. organization: Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, Alabama 35294 – sequence: 7 givenname: R. surname: Padmanabhan fullname: Padmanabhan, R. email: rp55@georgetown.edu organization: Department of Microbiology and Immunology, Georgetown University School of Medicine, Washington D. C. 20057 and |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/15917225$$D View this record in MEDLINE/PubMed |
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Snippet | Dengue virus type 2 (DEN2), a member of the Flaviviridae family, is a re-emerging human pathogen of global significance. DEN2 nonstructural protein 3 (NS3) has... |
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SubjectTerms | Acid Anhydride Hydrolases - metabolism Binding Sites Dengue Virus - enzymology Dengue virus type 2 Flaviviridae Kinetics Multiprotein Complexes Nucleoside-Triphosphatase - metabolism RNA Helicases - metabolism RNA-Dependent RNA Polymerase - metabolism Serine Endopeptidases - metabolism Viral Nonstructural Proteins - metabolism |
Title | Modulation of the Nucleoside Triphosphatase/RNA Helicase and 5′-RNA Triphosphatase Activities of Dengue Virus Type 2 Nonstructural Protein 3 (NS3) by Interaction with NS5, the RNA-dependent RNA Polymerase |
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