Inside the Viral Arms Race: Hampton University Student Explores How Viruses Outsmart the Immune System
HAMPTON, VA — On her first day at UC Berkeley’s Innovative Genomics Institute, Nurashau Blount walked into a lab known for pushing the boundaries of biology. Just a few doors down, Nobel laureate Dr. Jennifer Doudna, famous for co-developing CRISPR gene editing, was leading research that reshaped the way scientists think about DNA itself.
For Blount, a student at Hampton University studying biology, it was both intimidating and exhilarating, as she contributed to a project that probed another frontier of molecular biology: how viruses evolve to outsmart the very systems designed to stop them.
Working under Doudna and her team, Blount helped uncover a diverse family of viral enzymes called phosphodiesterases (PDEs), which allow viruses to evade immune detection, shutting down the cell’s internal communication network. Published in a preprint, “Divergent Viral Phosphodiesterases for Immune Signaling Evasion,” the study revealed that viruses across species use these enzymes to silence immune defences, offering insight into the evolutionary arms race between viruses and their hosts.
Blount sat down with us to discuss her summer lab experience.
Q&A with Nurashau Blount
Could you describe your specific role on the project and one major challenge you faced?
As an intern, my first task was to understand how the viral phosphodiesterase interacts with oligonucleotides, the small molecules that help maintain cell balance and immune response. My role focused on visualizing these interactions to help the team predict how the enzyme behaves in other contexts.
And, adjusting to such a research-intensive environment was definitely a challenge at first. I went from lab work two days a week at school to a full-time research setting surrounded by Ph.D. students and postdocs. But once I found my rhythm, I fell in love with the process of discovery.
What observation triggered this line of investigation into viral evasion via phosphodiesterases?
The project began when our team noticed a viral protein that was unusually selective in the way it cleared oligonucleotides. Typically, when viruses attack the cell’s defenses, they end updestroying essential molecules and killing the cell, which kills the virus, too. But this enzymeseemed to avoid that problem. It could destroy the immune-signaling molecules while leavingthe cell’s vital components intact. That kind of precision was fascinating and suggested that thevirus had evolved a more efficient survival mechanism.
How did your team uncover new PDE families that were previously unknown?
We used advanced computational modeling tools to predict the 3D structures of proteins acrossmultiple viral genomes. Traditional genetic methods would have missed these because theirsequences look so different, but structure prediction revealed that many unrelated viruses shared similar molecular folds. That told us these enzymes likely evolved separately to perform the same job.
The fact that so many distinct viruses developed this strategy shows how effective it is. It’s a reminder that evolution often reuses the same ideas, even in different organisms. And now that we can spot those patterns, we can start anticipating where they’ll show up next.
What are the next steps in this line of research? Could this lead to new antiviral therapies?
The next step is to capture the viral enzyme and its oligonucleotide target together to take asnapshot of their interaction. Once we can see exactly how the enzyme “grips” its target, we candesign molecules that block that interaction. Those inhibitors could form the basis of newantiviral drugs.
Beyond drug development, this work could also help scientists predict which viruses are mostlikely to evolve similar immune-evasion mechanisms. If we can identify those early, we canrespond faster to emerging viral threats.
What was your most exciting moment during the project?
One of the highlights for me was successfully purifying a protein sample to near perfection andthen watching it crystallize. In structural biology, you can’t see a protein’s detailed structurewithout those crystals. When I finally saw them form, I thought, This is it! This is what we’vebeen working toward. It was a small victory but an unforgettable one.
How did this experience shape your perspective on research?
It gave me a real sense of how much patience and creativity science demands. Everyexperiment builds on the last, often in ways that aren’t immediately obvious. I started toappreciate how viruses evolve these complex systems to survive and how researchers have to be just as creative to stay one step ahead.
Through this project, I also realized how deeply interconnected biology is. A single enzyme can tell a story about survival, adaptation, and even the history of disease. That realization made me want to keep studying structural biology and immunology, not just to understand how life works, but to find ways to protect it.
