Scientists have decoded the full 3D architecture of the flu’s (influenza virus) ribonucleoprotein (RNP) complex — a key machinery behind viral genome replication. This could pave the way for next-gen antivirals.
🔬🦠 Published in Science.
Unlike flu surface proteins (targets of most vaccines/drugs), RNP components are conserved and stable, making them ideal for broad-spectrum therapies.
Each RNP =
🧬 Viral RNA
🔗 Nucleoproteins (NPs)
🧰 A polymerase engine that copies RNA in host cells
🔍 Using cryo-electron microscopy & tomography, Peng et al. visualized the influenza RNP in atomic detail.
The structure?
➡️ A right-handed, antiparallel double helix
➡️ RNA nestled in the minor groove
➡️ NP subunits linked by a flexible tail loop
They captured the polymerase in action — in both preinitiation and elongation modes.
Key finding: The polymerase slides along the helical RNA strand without disrupting the RNP’s shape.
🧵Think: RNA copying on a conveyor belt that never stops moving.
This sliding mechanism is powered by the flexible NP tail loop, acting like molecular hinges.
It allows motion with low energy cost, aiding processivity and possibly helping the virus evade immune detection.
💊 Here’s the translational gold:
Using virtual screening, they found compounds that block the NP tail loop interface — disrupting the RNP’s assembly/function.
These leads inhibited virus replication in cells.
A promising antiviral target is born.
📌 Why it matters:
- Offers a new class of drug targets beyond fast-mutating surface proteins
- Provides a template for pan-influenza therapeutics
- Unlocks understanding of RNA virus replication machinery
This work highlights how marrying advanced structural biology with rational drug design can crack open viral secrets.
Congrats to Peng et al. for this milestone. A big leap in flu research.
📄 Science article
