Inhibition studies of methyltransferase domain of dengue virus protein NS-5 by a poly herbal extract- An Insilico Apporach.

2020 ◽  
Vol 9 (2) ◽  
pp. 69
Author(s):  
Vishwa Manivasagam ◽  
Padmini E
Keyword(s):  
Dengue Virus ◽  
Herbal Extract ◽  
Virus Protein ◽  
Methyltransferase Domain ◽  
Inhibition Studies

scholarly journals The methyltransferase domain of dengue virus protein NS5 ensures efficient RNA synthesis initiation and elongation by the polymerase domain

2015 ◽  
Vol 44 (6) ◽  
pp. 2974-2974 ◽  
Author(s):  
Supanee Potisopon ◽  
Stéphane Priet ◽  
Axelle Collet ◽  
Etienne Decroly ◽  
Bruno Canard ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Rna Synthesis ◽  
Virus Protein ◽  
Polymerase Domain ◽  
Methyltransferase Domain

scholarly journals The methyltransferase domain of dengue virus protein NS5 ensures efficient RNA synthesis initiation and elongation by the polymerase domain

2014 ◽  
Vol 42 (18) ◽  
pp. 11642-11656 ◽  
Author(s):  
Supanee Potisopon ◽  
Stéphane Priet ◽  
Axelle Collet ◽  
Etienne Decroly ◽  
Bruno Canard ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Rna Synthesis ◽  
Rna Binding ◽  
De Novo ◽  
Rna Virus ◽  
Single Strand ◽  
Virus Protein ◽  
Rdrp Activity ◽  
Polymerase Domain ◽  
Methyltransferase Domain

Abstract Viral RNA-dependent RNA polymerases (RdRps) responsible for the replication of single-strand RNA virus genomes exert their function in the context of complex replication machineries. Within these replication complexes the polymerase activity is often highly regulated by RNA elements, proteins or other domains of multi-domain polymerases. Here, we present data of the influence of the methyltransferase domain (NS5-MTase) of dengue virus (DENV) protein NS5 on the RdRp activity of the polymerase domain (NS5-Pol). The steady-state polymerase activities of DENV-2 recombinant NS5 and NS5-Pol are compared using different biochemical assays allowing the dissection of the de novo initiation, transition and elongation steps of RNA synthesis. We show that NS5-MTase ensures efficient RdRp activity by stimulating the de novo initiation and the elongation phase. This stimulation is related to a higher affinity of NS5 toward the single-strand RNA template indicating NS5-MTase either completes a high-affinity RNA binding site and/or promotes the correct formation of the template tunnel. Furthermore, the NS5-MTase increases the affinity of the priming nucleotide ATP upon de novo initiation and causes a higher catalytic efficiency of the polymerase upon elongation. The complex stimulation pattern is discussed under the perspective that NS5 adopts several conformations during RNA synthesis.

Recognition of Dengue Virus Protein Using Epitope-Mediated Molecularly Imprinted Film

2005 ◽  
Vol 77 (16) ◽  
pp. 5140-5143 ◽  
Author(s):  
Dar-Fu Tai ◽  
Chung-Yin Lin ◽  
Tzong-Zeng Wu ◽  
Li-Kuang Chen
Keyword(s):  
Dengue Virus ◽  
Virus Protein ◽  
Molecularly Imprinted ◽  
Molecularly Imprinted Film

scholarly journals Studi in Silico Lima Senyawa Aktif Sebagai Penghambat Protein Virus Dengue

2019 ◽  
pp. 40-47
Author(s):  
Reni Herman
Keyword(s):  
Dengue Virus ◽  
In Silico ◽  
Dengue Infection ◽  
Epigallocatechin Gallate ◽  
Denv Infection ◽  
Virus Protein ◽  
Structural Protein ◽  
The Stability ◽  
The Tropics ◽  
Ns3 Protease

Dengue infection is an endemic disease in the tropics and subtropics, caused by dengue virus (DENV) infection. Some compounds have been shown to have antiviral effects on some viruses. In silico study is conducted to predict the stability of natural ingredient compounds: artemisinin, catechin, mangiferin, epigallocatechin gallate (EGCG), and quercetin in their interactions with dengue virus proteins at molecular level. This study is carried out using the 2008 version of the Molecular Operating Environment (MOE) software. Ligands are ribavirin as antiviral control whereas artemisinin, mangiferin, EGCG, and quercetin with 3D mole format structures. The downloaded DENV protein with PDB document format is the DENV serotype 2 envelope protein with 1OKE code, non structural protein 3 (NS3) with 2VBC code and NS5 protein with 1L9K code. In silico test generally showed that catechin, mangiferin, EGCG, and quercetin had more stable docking ligands to DENV’s proteins. In particular, mangiferin had stable docking ligand to envelope proteins, NS3 (helicase and protease) and in NS5-methyltransferase compared to ribavirin. Catechin stabled on NS3-protease, EGCG on NS3 (helicase and protease) and quercetin on NS3-protease. Artemisinin had less stabled bonds than ribavirin. The results indicated that catechin, mangiferin, EGCG, and quercetin had potential inhibition to DENV proteins whereas mangiferin was the most potential compound to inhibit dengue virus protein targets.

scholarly journals Molecular Basis of Differential Stability and Temperature Sensitivity of ZIKA versus Dengue Virus Protein Shells

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Chinmai Pindi ◽  
Venkat R. Chirasani ◽  
Mohammad Homaidur Rahman ◽  
Mohd Ahsan ◽  
Prasanna D. Revanasiddappa ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Temperature Sensitivity ◽  
Molecular Basis ◽  
Virus Protein ◽  
Differential Stability

scholarly journals Dengue Virus Type 2: Protein Binding and Active Replication in Human Central Nervous System Cells

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Ma Isabel Salazar ◽  
Marissa Pérez-García ◽  
Marisol Terreros-Tinoco ◽  
María Eugenia Castro-Mussot ◽  
Jaime Diegopérez-Ramírez ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Dengue Virus ◽  
Protein Binding ◽  
Gray Matter ◽  
Primary Cultures ◽  
Virus Protein ◽  
Specific Marker ◽  
Human Central Nervous System ◽  
Human Neurons

An increased number of dengue cases with neurological complications have been reported in recent years. The lack of reliable animal models for dengue has hindered studies on dengue virus (DENV) pathogenesis and cellular tropismin vivo. We further investigate the tropism of DENV for the human central nervous system (CNS), characterizing DENV interactions with cell surface proteins in human CNS cells by virus overlay protein binding assays (VOPBA) and coimmunoprecipitations. In VOPBA, three membrane proteins (60, 70, and 130 kDa) from the gray matter bound the entire virus particle, whereas only a 70 kDa protein bound in white matter. The coimmunoprecipitation assays revealed three proteins from gray matter consistently binding virus particles, one clearly distinguishable protein (~32 kDa) and two less apparent proteins (100 and 130 kDa). Monoclonal anti-NS3 targeted the virus protein in primary cell cultures of human CNS treated with DENV-2, which also stained positive for NeuH, a neuron-specific marker. Thus, our results indicate (1) that DENV-2 exhibited a direct tropism for human neurons and (2) that human neurons sustain an active DENV replication as was demonstrated by the presence of the NS3 viral antigen in primary cultures of these cells treated with DENV-2.

Label-free electrical recognition of a dengue virus protein using the SEGFET simplified measurement system

2014 ◽  
Vol 6 (22) ◽  
pp. 8882-8885 ◽  
Author(s):  
Nirton C. S. Vieira ◽  
Alessandra Figueiredo ◽  
Juliana F. dos Santos ◽  
Ségio M. Aoki ◽  
Francisco E. G. Guimarães ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Measurement System ◽  
Field Effect ◽  
Field Effect Transistor ◽  
Nonstructural Protein ◽  
Virus Protein ◽  
Label Free ◽  
Nonstructural Protein 1 ◽  
System P ◽  
Effect Transistor

Separative extended gate field-effect transistor was applied as an immunosensor for the label-free recognition of dengue virus nonstructural protein 1 (NS1).

scholarly journals The RNA helicase, nucleotide 5′-triphosphatase, and RNA 5′-triphosphatase activities of Dengue virus protein NS3 are Mg2+-dependent and require a functional Walker B motif in the helicase catalytic core

Virology ◽  
2004 ◽  
Vol 328 (2) ◽  
pp. 208-218 ◽  
Author(s):  
Delphine Benarroch ◽  
Barbara Selisko ◽  
Giada A. Locatelli ◽  
Giovanni Maga ◽  
Jean-Louis Romette ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Rna Helicase ◽  
Virus Protein ◽  
Catalytic Core
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