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Last update 08 May 2025

VP24

Last update 08 May 2025

Basic Info

Synonyms

Ebola VP24, eVP24, Membrane-associated protein VP24

+ [1]

Introduction

Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways. Blocks the IFN-induced nuclear accumulation of host phosphorylated STAT1 by interacting with the STAT1-binding region of host importins. Alternatively interacts also directly with host STAT1 and may additionally inhibit its non-phosphorylated form. Plays a role in assembly of viral nucleocapsid and virion budding. May act as a minor matrix protein that plays a role in assembly of viral nucleocapsid and virion budding.

Drugs associated with VP24

AVI-7537

Target

VP24 x Viral RNA

Mechanism

Viral RNA inhibitors [+2]

Active Org.-

Originator Org.

Sarepta Therapeutics, Inc.

Active Indication-

Inactive Indication

Hemorrhagic Fever, Ebola

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

AVI-6003

Target

VP24

Mechanism

VP24 inhibitors

Active Org.-

Originator Org.

Sarepta Therapeutics, Inc.

Active Indication-

Inactive Indication

Marburg Virus Disease

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with VP24

NCT01593072

/ WithdrawnPhase 1

A Randomized, Double-Blind, Placebo-Controlled, Multiple-Dose, Dose-Escalation A Randomized, Double-Blind, Placebo-Controlled, Multiple-Dose, Dose-Escalation Study to Assess the Safety, Tolerability and Pharmacokinetics of AVI-7537 in Healthy Adult Volunteers

The purpose of this study is to evaluate the safety and tolerability of healthy male and female subjects with intravenous (IV) infusions of AVI 7537 compared to matched placebo in and to evaluate the pharmacokinetics (PK).

Start Date01 Aug 2012

Sponsor / Collaborator

Sarepta Therapeutics, Inc.

NCT01353040

/ CompletedPhase 1

A Randomized, Double-Blind, Placebo-Controlled, Single-Dose, Dose-Escalation Study to Assess the Safety, Tolerability and Pharmacokinetics of AVI-6003 in Healthy Adult Volunteers

The purpose of this study is to characterize the safety and pharmacology of single administrations of AVI-6003, a post-exposure prophylaxis candidate treatment for Marburg virus.

Start Date01 May 2011

Sponsor / Collaborator

Sarepta Therapeutics, Inc.

100 Clinical Results associated with VP24

100 Translational Medicine associated with VP24

0 Patents (Medical) associated with VP24

220

Literatures (Medical) associated with VP24

01 May 2025·Journal of Molecular Graphics and Modelling

Computational study of interaction of calixarene with ebola virus structural proteins and its potential therapeutic implications

Article

Author: Maity, Atanu ; Dutta, Tanmoy ; Alomary, Mohammad N ; Alharbi, Ali H ; Jamal, Qazi Mohammad Sajid ; Jamous, Yahya F ; Ahmad, Varish ; Ansari, Mohammad Azam

Ebola virus (EBOV) is a negative-strand RNA virus that causes hemorrhagic fever and fatal illness in humans. According to WHO, the Ebola virus caused 28,646 fatal cases and 11,323 deaths in West Africa due to hemorrhagic fever and deadly disease in humans between 2013 and 2016. Between 1976 and 2022, approximately 15,409 fatalities caused by EBOV took place worldwide. Unfortunately, no effective vaccine or drugs are available to prevent this deadly disease. In the present study, State-of-the-art tools based on in-silico methods were used to elucidate the interaction pattern of calixarene (CAL) with seven EBOV structural proteins, i.e., GP1,2, nucleoprotein (NP), polymerase cofactor (VP35), (VP40), transcription activator (VP30), VP24, and RNA-dependent RNA polymerase (L). CAL is a cage-like compound with supramolecular features. The molecular docking lead analysis using AutoDock tool has been performed to find out the binding pattern of CAL with EBOV proteins. Obtained results revealed efficient inhibitory properties of calixarene (CAL) against seven Ebola virus structural proteins i.e., GP1,2, nucleoprotein (NP), polymerase cofactor (VP35), (VP40), transcription activator (VP30), VP24, and RNA-dependent RNA polymerase (L). Molecular docking analysis shows that the interaction of CAL with VP24 was highest with the total binding energy -12.47 kcal/mol and 26.90 nM inhibitions constant. Molecular Dynamics study has also quantified the efficiency of CAL against VP24. In conclusion, the present study suggests that CAL and its derivatives could be used as inhibitors to counter EBOV infection. Furthermore, in vitro and in vivo laboratory experimentation is required to establish CAL and its derivatives as a potential inhibitor against EBOV.

18 Mar 2025·Journal of Virology

Class B scavenger receptor resists WSSV replication by recognizing the viral lipid molecule and promoting phagocytosis

Article

Author: Yang, Hui-Ting ; Guo, Xin-Lu ; Huang, Yi-Heng ; Shan, Meng-Ke ; Yang, Gui-Wen

ABSTRACT Class B scavenger receptors (SRBs) have been well-studied in bacteria-induced immune responses in invertebrates. However, the status of SRB-defending viruses remains unclear. In this study, we identified a scavenger receptor in Procambarus clarkii (crayfish), which is homologous to mammalian SRBs, and designated it as Pc SRB. The expression of Pc SRB was upregulated after the WSSV challenge. The survival rate of crayfish was decreased, but the WSSV copy number increased after Pc SRB knockdown during virus invasion. In addition, Pc SRB bound to WSSV. Furthermore, we detected how Pc SRB interacted with WSSV, and we found that Pc SRB could bind to cholesta-3,5-diene, (CD3,5), a novel WSSV lipid ligand, rather than dibutyl phthalate (DBP). Besides, Pc SRB could bind to VP19, VP26, and VP28, rather than VP24. Mutant-binding experiments demonstrated that the hydrophobic domain (130–180 aa) of Pc SRB is important for recognizing WSSV. Furthermore, Pc SRB might promote lysosomal eliminating function to degrade WSSV. Altogether, we identified a new mechanism for scavenger receptor recognition and resistance to WSSV. IMPORTANCEPc SRB could bind to WSSV directly. Pc SRB could interact with WSSV via binding to lipid molecule CD3,5 and viral envelope proteins. Pc SRB could influence lysosomal activation.

01 Feb 2025·Journal of Infection and Public Health

Discovery of anti-Ebola virus multi-target inhibitors from traditional Chinese medicine database using molecular screening, biophysical investigation, and binding free energy calculations

Article

Author: Agouni, Abdelali ; Sayaf, Abrar Mohammad ; Wei, Dong-Qing ; Alshabrmi, Fahad M ; Mohammad, Anwar ; Khan, Abbas ; Benameur, Tarek ; Yeoh, Kar Kheng

INTRODUCTIONEbola virus (EBOV) is a highly lethal RNA virus that causes severe hemorrhagic fever in humans and non-human primates. The lack of effective treatment or vaccine for this pathogen poses a serious threat to a global pandemic. Therefore, it is imperative to explore new drugs and therapies to combat this life-threatening infection.MATERIALS AND METHODSIn this study, we employed in silico methods to assess the inhibitory activity of natural products from traditional Chinese medicine (TCM) against four EBOV proteins that are crucial for viral replication and assembly: VP40, VP35, VP30, and VP24. We performed molecular docking of TCM compounds with the EBOV proteins and screened them based on their docking scores, binding free energies, and pharmacokinetic properties.RESULTSOur results pinpointed eight TCM compounds (TCM1797, TCM2872, TCM250, TCM2837, TCM2644, TCM4697, TCM2322, and TCM277) that exhibited superior efficacy in inhibiting all the EBOV proteins compared to the controls. These compounds interacted with key residues of the EBOV proteins through various types of bonds, such as hydrogen bonds, salt bridges, and π-π interactions, forming stable complexes that could disrupt the function of the EBOV proteins. These compounds were found to possess known antiviral activity, acceptable pharmacokinetic properties, and human usage history, which make them promising candidates for anti-EBOV drug development. Moreover, the molecular simulation analysis confirmed the binding stability, structural compactness, and residue flexibility properties of these compounds. Furthermore, the binding free energy results revealed that VP30-TCM2644, VP30-TCM4697, VP35-TCM2837, VP24-TCM250, and VP24-TCM277 complexes exhibit significant binding free energy values compared to the control ligands. Principal Component Analysis (PCA) and Free Energy Landscape (FEL) results revealed the trajectories' motion and conformational energy states.CONCLUSIONSOur findings provide valuable insights into the molecular mechanisms driving the efficacy of TCM drugs against EBOV and suggest novel approaches for the development of anti-EBOV therapies.

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VP24

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