Last update 01 Nov 2024

dengue E protein

Last update 01 Nov 2024

Basic Info

Synonyms-

Introduction-

Drugs associated with dengue E protein

VIS-513

Target

dengue E protein

Mechanism

dengue E protein inhibitors

Active Org.

Visterra, Inc.

Originator Org.

Visterra, Inc.

Active Indication

Dengue

Inactive Indication-

Drug Highest PhasePhase 2

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with dengue E protein

NCT06551844 / Not yet recruitingPhase 2IIT

Adaptive Dengue Antiviral Platform Trial (ADAPT): a Phase 2 Randomized, Adaptive, Open Label Trial for Antiviral Screening in Patients With Early Symptomatic Dengue

This is a randomized, open-label adaptive platform trial aiming to screen the antiviral effectiveness of the experimental drug(s) in early dengue infection
* Primary objectives:
* To determine the antiviral effectiveness of the experimental drug(s) in early dengue infection
* To assess the safety and tolerability of the experimental drug(s) in dengue patients
* Secondary objective:
* To assess the effect of the experimental drug(s) in dengue patients on physiological, clinical and virological parameters

Start Date01 Sep 2025

Sponsor / Collaborator

Oxford University Clinical Research Unit, Vietnam

[+1]

100 Clinical Results associated with dengue E protein

100 Translational Medicine associated with dengue E protein

0 Patents (Medical) associated with dengue E protein

Literatures (Medical) associated with dengue E protein

01 Jan 2023·Journal of Vector Borne Diseases

Epitope prediction and designing of receptor inhibitor of Dengue Envelope Protein: An in silico approach

Article

Author: Kumari, Ankita ; Singh, Karuna ; Uttam, Gunjan

BACKGROUND & OBJECTIVESDengue virus (DENV) is the causative agent of dengue fever (DF) and dengue hemorrhagic fever (DHF). It has four distinct serotypes (DENV-1, DENV-2, DENV-3, and DENV-4) based on their antigenic properties. Mostly, the immunogenic epitopes are present in the envelope (E) protein of the virus. Heparan sulfate (HS) acts as a receptor and interacts with the E protein of the virus thus facilitating the entry of dengue virus into human cells. This study focuses on epitope prediction on the E protein of the DENV serotype. The non-competitive inhibitors of HS were designed using bioinformatics.METHODSIn the present study, epitope prediction of the E protein of DENV serotypes was performed using the ABCpred server and IEDB analysis resource. The interactions of HS and viral E proteins (PDB ID: 3WE1 and PDB ID:1TG8) were evaluated through AutoDock. Subsequently, non-competitive inhibitors were designed to bind the E protein of DENV better than HS. All the docking results were validated by re-docking the ligand-receptor complexes and superimposing them onto their co-crystallized complexes using AutoDock and visualizing them in Discovery Studio.RESULTSThe result predicted B-cell and T-cell epitopes on the E protein of DENV serotypes. The designed HS ligand 1 (non-competitive inhibitor) demonstrated potential binding with the DENV E protein, thereby inhibiting HS-E protein binding. The re-docked complexes were superimposed entirely onto the native co-crystallized complexes (low root mean square deviation values), which validates the docking protocols.INTERPRETATION & CONCLUSIONThe identified B-cell and T-cell epitopes of the E protein and non-competitive inhibitors of HS (ligand 1) could be used in the designing of potential drug candidates against the dengue virus.

01 Feb 2022·Mini-Reviews in Medicinal ChemistryQ3 · MEDICINE

Dengue Virus Entry/Fusion Inhibition By Small Bioactive Molecules: A Critical Review

Q3 · MEDICINE

Review

Author: Pottabatula, Shyam Sunder ; Jubie, Selvaraj ; Naresh, Podila

:Many flaviviruses are remarkable human pathogens that can be transmitted by mosquitoes and ticks. Despite the availability of vaccines for viral infections such as yellow fever, Japanese encephalitis, and tick-borne encephalitis, flavivirus-like dengue is still a significant life-threatening illness worldwide. To date, there is no antiviral treatment for dengue therapy. Industry and the research community have been taking ongoing steps to improve anti-flavivirus treatment to meet this clinical need. The successful activity has been involved in the inhibition of the virus entry fusion process in the last two decades. In this study, the latest understanding of the use of small molecules used as fusion inhibitors has been comprehensively presented. We summarized the structure, the process of fusion of dengue virus E protein (DENV E), and the amino acids involved in the fusion process. Special attention has been given to small molecules that allow conformational changes to DENV E protein, viz. blocking the pocket of βOG, which is important for fusion.

01 Dec 2021·Bioorganic & Medicinal ChemistryQ3 · MEDICINE

Peptidomimetic analogues of an Arg-Trp-x-x-Trp motif responsible for interaction of translocase MraY with bacteriophage ϕX174 lysis protein E

Q3 · MEDICINE

Article

Author: Fairbairn, Julia A ; Kerr, Rachel V ; Merritt, Andrew T ; Bugg, Timothy D H

Translocase MraY is the target for bacteriophage ϕX174 lysis protein E, which interacts via a protein-protein interaction mediated by Phe-288 and Glu-287 of E. coli MraY, and an Arg-Trp-x-x-Trp motif on protein E, also found in several cationic antimicrobial peptides. Analogues of Arg-Trp-octyl ester, found previously to show antimicrobial activity, were tested for antimicrobial activity, with Lys-Trp-oct (MIC₅₀P. fluorescens 5 µg/mL) and Arg-Trp-decyl ester (MIC₅₀P. fluorescens 3 µg/mL) showing enhanced antimicrobial activity. Synthesis and testing of α-helix peptidomimetic analogues for this motif revealed improved antibacterial activity (MIC₅₀E. coli 4-7 µg/mL) for analogues containing two aromatic substituents, mimicking the Arg-Trp-x-x-Trp motif, and MraY inhibition (IC₅₀ 140 µM) by one such peptidomimetic. Investigation of mechanism of action using the Alamar Blue membrane permeabilisation assay revealed bacteriostatic and bacteriocidal mechanisms in different members of this set of compounds, raising the possibility of more than one biological target. The observed antimicrobial activity and MraY inhibition shown by peptidomimetic compounds confirms that this site could be targeted by drug-like molecules.

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dengue E protein

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