N-terminal lysine as a critical determinant of odilorhabdin susceptibility to inactivation by the self-resistance acetyltransferase OatA
Emilie Racine, Anne Lanois-Nouri, Jessica Houard, Lucile Pantel, Alain Givaudan, Maxime Gualtieri · 2026
Read N-terminal lysine as a critical determinant of odilorhabdin susceptibility to inactivation by the self-resistance acetyltransferase OatA by Emilie Racine, Anne Lanois-Nouri, Jessica Houard, Lucile Pantel, Alain Givaudan, Maxime Gualtieri (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13689418.txt.
Description
Emilie Racine and co-authors pinpoint the single amino acid that lets a bacterium's own enzyme disarm its antibiotic, and show that swapping it foils the defense, in work from twenty twenty-six. Odilorhabdins kill bacteria by jamming their ribosomes. The producing bacterium protects itself with an enzyme that tags the drug and kills its power.
A scan swapping one residue at a time flagged the first lysine as the tag target. When the enzyme was switched on in test bacteria, the natural drug's strength fell sixty-four fold. The swapped variant stayed almost fully untagged after hours and kept killing. The enzyme ignored other common antibiotics. Design rules for tougher versions follow.
Catalog record
| CREATOR | Emilie Racine, Anne Lanois-Nouri, Jessica Houard, Lucile Pantel, Alain Givaudan, Maxime Gualtieri |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 36 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |