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The system that edits viral RNA rather than cutting it.
Complexe RdrA-D dont RdrB est une désaminase A→I (adénosine→inosine) homologue à ADAR1 humain. L'édition massive de l'ARN viral le paralyse. Cible directe pour la pharmacologie des interféronopathies (Aicardi-Goutières) et des antiviraux ARN.
Cutting viral RNA has become a classic of bacterial defenses (RNase III, CRISPR-Cas13). But RADAR does something more subtle: it edits viral RNA, converting adenosines into inosines (which are read as guanines). The result? The phage transcript changes meaning, the proteins produced are misfolded or non-functional, and the phage aborts without a single strand of DNA being cleaved. Subtle, irreversible, elegant. And the most striking part: it's exactly the same chemistry as human ADAR1 — except ADAR1 does the opposite (edits endogenous RNA to hide it from the immune system). Same enzyme, two opposite uses.
The RADAR → ADAR1 lead is our best shot at attacking human ADAR1 selectively. Overexpressed ADAR1 lets tumors and HIV hide their double-stranded RNA from the immune system — so inhibiting it means reawakening the endogenous antiviral response.
The cryo-EM assembly of RADAR published in 2023 looks like a watch gear wheel — a helical filament made of the ATPase RdrA and the deaminase RdrB self-assembling together. It is one of the most beautiful supramolecular enzyme complexes ever characterized.
