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Canonical sources

Bactaegion does not duplicate any scientific data. Everything comes from public databases.

★ Curated sources
🔍 Search public databases
Protein domains
📚 Reference bibliography
Bernheim A. et al., Prokaryotic viperins produce diverse antiviral molecules, Nature 589 (2021). doi:10.1038/s41586-020-2762-2
Lachowicz J.C. et al., Discovery of a homologous family of antiviral nucleotide analogs, ACS Cent. Sci. 8 (2022).
★ Princeps publication
Bernheim et al. (2021). Prokaryotic viperins produce diverse antiviral molecules. Nature.

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1-21 · canonical · series 2026/2

Viperines

Bacterial viperin — antiviral nucleotide analogs

The system that copies human recipes, only simpler.

Viperin bactérienne (bVip) convertit CTP/UTP/GTP en analogues ddh-NTP, terminateurs de chaîne contre l'ARN polymérase virale. Même chimie que Sofosbuvir (anti-VHC Gilead, ~30 Md$ de ventes). Précurseur évolutif naturel d'un blockbuster pharmaceutique majeur.

Proteins
12
Host
bactéries
Discovery
Bernheim A., 2021
Mechanism
enzyme radical-SAM → ddh-NTP
EXPLORE 12 PROTEINS OPEN THE LIBRARY frame a hypothesis →
Also documented in the V1 library see the full entry →
✦ The story

For two decades, RSAD2 ("Viperin") was a revered mystery among human immunologists: an interferon-induced gene that slows down HIV, HCV, flaviviruses, and even a few coronaviruses, but whose mechanism nobody could pin down. Then Aude Bernheim looked at bacteria. In 2021, her team showed that hundreds of bacteria carry a homolog doing exactly the same thing against phages: producing chain-terminator nucleotides (ddhCTP / ddhGTP). Once identified in the bacterium, the mechanism became obvious in humans — and the bacterial version provided a simpler structural model to crystallize and use as a scaffold for molecule optimization.

Discovered 2021
By Bernheim, Millman, Sorek, Pinilla-Redondo et al. (Weizmann + INSERM + Copenhagen)
★ Why we care

ddhCTP is a natural broad-spectrum antiviral. Chemically stabilized (resistant to the phosphatases that normally degrade it within minutes in plasma), it is a credible drug candidate. And the bacterial version remains the best structural template for design.

◇ The detail that lands

The name "viperin" was coined in 1995 as an acronym for virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible — five adjectives crammed together. The bacterial version dropped the "endoplasmic reticulum" (bacteria don't have one) but kept everything else. Science is rarely this economical with its vocabulary.

3D structure · AlphaFold
bVip (Viperin Rhodococcus) · A0A1H6JLW8
open on alphafold.ebi.ac.uk ↗UniProt entry ↗
Model fetched live from AlphaFold-EBI · CC BY 4.0 · structure never stored by Bactaegion
↗ Cross-reading — Wikipedia
CC BY-SA · live fetch, never stored by Bactaegion

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Sources
  1. Bernheim A. et al., Prokaryotic viperins produce diverse antiviral molecules, Nature 589 (2021). doi:10.1038/s41586-020-2762-2
  2. Lachowicz J.C. et al., Discovery of a homologous family of antiviral nucleotide analogs, ACS Cent. Sci. 8 (2022).
Open leads on Viperines · 2
Analogues ddhCTP optimisés pour flavivirus (Zika, dengue)
pre-clinical 7 contrib.
bVip-RSAD2 chimère → activation interféron-indépendante
in progress 4 contrib.