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Updated: Jul 22, 2025
High-throughput Screening for Broad-spectrum Chemical Inhibitors of RNA Viruses
Published on: May 5, 2014
Exploring the chemical space for potential inhibitors against cell surface binding protein of Mpox virus using
Dwaipayan Chaudhuri1, Satyabrata Majumder1, Joyeeta Datta1
1Department of Life Sciences, Presidency University, Kolkata, India.
Abstract:
Mpox virus is the latest member of the Poxviridae family of which small pox virus is a member. Monekypox virus has led to thousands of infections across the globe. Poxvirus gains entry into the cell making use of glycosaminoglycans like chondroitin sulphate and heparan sulphate. The interaction of the Mpox virus protein E8L also called cell surface binding protein is crucial for host cell attachment, membrane fusion and viral entry into the host cell leading to establishment of infection thus making this protein a very attractive therapeutic target. In this study we have tried to utilize the chondroitin sulphate binding groove present in the protein and identify molecules which are structurally similar to chondroitin sulphate. These molecules can thus occupy the same pocket but with a better binding affinity than chondroitin sulphate in order to outcompete the latter molecule from binding to the E8L protein and thus prevent it from performing its function. This study may pave the way for development of highly efficient therapeutics against the Mpox virus and further curb its infective potential.Communicated by Ramaswamy H. Sarma.
Insights
Researchers identified molecules that bind to the Mpox virus E8L protein, blocking viral entry. This discovery offers a promising strategy for developing new therapeutics against the Mpox virus.
Area of Science:
- Virology
- Molecular Biology
- Drug Discovery
Background:
- Mpox virus, a member of the Poxviridae family, has caused global infections.
- Poxviruses enter cells using glycosaminoglycans, such as chondroitin sulfate and heparan sulfate.
- The Mpox virus E8L protein (cell surface binding protein) is critical for host cell attachment and viral entry.
Purpose of the Study:
- To identify novel molecules that can inhibit Mpox virus infection.
- To target the chondroitin sulfate binding groove of the E8L protein.
- To develop potential therapeutics by outcompeting natural ligands for E8L binding.
Main Methods:
- Structural analysis of the chondroitin sulfate binding groove in the Mpox virus E8L protein.
- In silico identification of molecules structurally similar to chondroitin sulfate.
- Evaluating the binding affinity of identified molecules to the E8L protein.
Main Results:
- Molecules with higher binding affinity to the E8L protein's chondroitin sulfate binding groove were identified.
- These molecules have the potential to block viral attachment and entry.
- The study provides a foundation for developing novel anti-Mpox virus therapeutics.
Conclusions:
- Targeting the E8L protein's binding pocket with high-affinity molecules is a viable therapeutic strategy.
- This approach could lead to effective treatments to curb the spread of Mpox virus infections.
- Further research may yield potent inhibitors for Mpox virus therapeutics.
