Nikhil Prasad Fact checked by:Thailand Medical News Team Oct 27, 2025 3 hours, 10 minutes ago
Medical News:
SARS-CoV-2 Hijacks Human Drosha Enzyme to Aid Its Own Survival
A new study led by scientists from West Virginia University has revealed that the COVID-19 virus (SARS-CoV-2) triggers a surprising molecular change inside lung cells. The virus alters a vital enzyme called Drosha—an RNase-III protein responsible for processing microRNAs that regulate genetic activity. This
Medical News report shows that when Drosha’s normal form is disrupted and replaced with smaller fragments, the virus’s ability to replicate becomes weaker.
Drosha Enzyme Shift Found to Weaken COVID-19 Virus Replication
The discovery provides a new perspective on how SARS-CoV-2 interacts with human cellular machinery. Drosha usually lives in the cell nucleus, where it helps manage RNA molecules. However, researchers found that during COVID-19 infection, the enzyme is cleaved into smaller versions—known as the P140 and P25 isoforms—and these pieces relocate to the cytoplasm, the cell’s outer region. This shift was not observed with other mild coronaviruses like HCoV-OC43 or HCoV-229E, suggesting this reaction is unique to SARS-CoV-2.
How the Study Was Conducted
Using advanced imaging and genetic tools, the scientists infected human lung epithelial cells (NuLi-1) with multiple SARS-CoV-2 variants, including Alpha and Beta. They observed that Drosha was not only broken down but also moved away from the nucleus. Further experiments using cells genetically engineered to lack Drosha showed that these cells produced significantly less viral RNA, confirming that the virus depends on Drosha for efficient replication.
Interestingly, the researchers also found that this process is not due to alternative splicing—a normal way cells generate protein variants—but rather to proteolytic cleavage, where Drosha is cut by specific enzymes. The team suspects that the virus may trigger human proteases or use its own proteases, such as Mpro or 3CLpro, to perform this cleavage.
Why This Matters
The finding highlights a hidden strategy used by SARS-CoV-2 to hijack the host’s RNA processing system. By forcing Drosha out of its usual place in the nucleus, the virus may interfere with the body’s normal gene regulation and immune defenses. This insight opens new doors for antiviral therapies that could block Drosha’s cleavage or prevent its cytoplasmic translocation, thereby slowing viral replication.
Implications for Future Coronavirus Research
The research also points to Drosha’s possible dual role—both as a guardian of cellular RNA integrity and, paradoxically, as a tool exploited by viruses. Since the study demonstrated that loss of Drosha weakens SARS-CoV-2 replication, targeting this enzyme’s interaction pathway could become a future therapeutic approach.
Conclusion
This pioneering study reveals that
SARS-CoV-2 manipulates Drosha, a key RNA-processing enzyme, by cleaving and relocating it within human lung cells. This alteration helps the virus replicate more effectively. Understanding this mechanism not only provides new insights into how COVID-19 undermines cellular defenses but also offers hope for new antiviral treatments that could interrupt this process. As viruses continue to evolve, studying how they exploit human molecular systems like Drosha will remain critical in preparing for future outbreaks.
The study findings were published in the peer reviewed journal: Genes.
https://www.mdpi.com/2073-4425/16/10/1239
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