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Medical News: New Hope for Dengue Treatment as Fruit Compound Blocks Key Viral Proteins
In a promising breakthrough, scientists from the School of Biotechnology at Gangadhar Meher University in India have identified a naturally occurring plant compound that may be able to stop the dengue virus from replicating. Using powerful computer simulations, the researchers found that a compound called naringenin, commonly found in citrus fruits like oranges and grapefruits, could interfere with the virus’s internal machinery—potentially paving the way for new antiviral drugs.
Scientists use computer simulations to show that citrus compound naringenin can block critical proteins
in the dengue virus and may serve as a new antiviral drug
This
Medical News report covers the important findings of this pioneering study, which targets a critical protein-protein interaction inside the dengue virus that is vital for its replication and survival.
Why Dengue Is Still a Global Threat
Dengue continues to be one of the most rapidly spreading mosquito-borne diseases in the world. According to the World Health Organization, as of April 2024, more than 7.6 million cases were reported globally. Currently, there are no approved direct-acting antiviral drugs specifically for dengue, making it a major challenge for doctors and health systems.
The dengue virus has four main types, and once a person gets infected with one type, they’re only immune to that specific one. A second infection with a different type often leads to more severe disease. This makes the search for broad-spectrum treatments even more urgent.
What the Scientists Targeted
The researchers focused on two dengue proteins—NS3 and NS4B—that play a central role in helping the virus multiply inside the body. These two proteins interact closely to assemble the replication complex, which is necessary for copying the virus’s genetic material.
Using advanced computer modeling and molecular simulations, the team found that naringenin fits snugly into a key site on the NS3 protein. This same site is where NS4B usually binds. If naringenin occupies this spot, NS4B cannot attach, disrupting the replication process.
Key Findings from the Study
Naringenin showed strong binding to three critical amino acids in the NS3 protein—Leu193, His194, and Ala197. These amino acids were also identified as being essential for NS4B’s interaction with NS3. By blocking this connection, naringenin could potentially “jam” the viral machinery.
To confirm the strength of the interaction, the researchers ran 50-nanosecond molecular dynamics simulations. These revealed that the bond between naringenin and NS3 remained stable throughout the simulated period. Even when mutations like G124A were introduced into the NS4B protein, the critical amino acids in NS3 still played a central role—suggesting naringenin might
work against both regular and mutated versions of the virus.
Further analysis using the ConSurf server confirmed that the three amino acids are highly conserved across different strains, meaning they are vital for the virus and unlikely to change over time—making them ideal drug targets.
Safety and Drug Potential
Naringenin also showed good drug-like properties in safety evaluations. It was predicted to be non-toxic, non-mutagenic, and not harmful to the liver or heart. It passed major drug-likeness filters and has decent oral bioavailability, making it a viable candidate for development as an oral medication.
Conclusion
This study presents strong computer-based evidence that the citrus compound naringenin can bind to and potentially block a crucial protein-protein interaction in the dengue virus. If these results are confirmed in laboratory and clinical studies, naringenin could lead to a new class of antiviral drugs for dengue—a disease that currently lacks specific treatments. Given its natural origin, low toxicity, and stable interaction with key viral proteins, naringenin stands out as a promising lead compound for future drug development.
The study findings were published in the peer reviewed journal: Discover Chemistry.
https://link.springer.com/article/10.1007/s44371-025-00409-3
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