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The tetracycline resistome is shaped by selection for specific resistance mechanisms by each antibiotic generation

Bacteria can use different mechanisms to become resistant to the same antibiotic class. Here, the authors study bacterial strains that express genes conferring tetracycline resistance via different mechanisms, and find that each mechanism is preferentially selected for by specific tetracycline generations.

Kevin S. Blake
Yao-Peng Xue
Gautam Dantas
ResearchOpen Access07 Feb 2025
Nature Communications

Volume: 16, P: 1-14
Plasticity, dynamics, and inhibition of emerging tetracycline resistance enzymes

Structural and functional characterization of tetracycline-inactivating enzymes reveals that inhibitors act by locking the enzyme in an unproductive state by restricting substrate-driven conformational dynamics that are important for catalysis.

Jooyoung Park
Andrew J Gasparrini
Niraj H Tolia
Research08 May 2017
Nature Chemical Biology

Volume: 13, P: 730-736
The structural basis of N-acyl-α-amino-β-lactone formation catalyzed by a nonribosomal peptide synthetase

The antimicrobial β-lactone obafluorin is produced by a Nonribosomal Peptide Synthetase (NRPS). Here the authors present the crystal structure of the obafluorin NRPS and develop a reconstitution assay that allows them to analyse product formation from obafluorin NRPS mutants and alternate substrates.

Dale F. Kreitler
Erin M. Gemmell
Andrew M. Gulick
ResearchOpen Access31 Jul 2019
Nature Communications

Volume: 10, P: 1-13
β-Lactone formation during product release from a nonribosomal peptide synthetase

In vitro reconstitution of five enzymes elucidates the biosynthetic pathway of obafluorin (Obi) and reveals that ObiF uses an unusual thioesterase domain to cyclize the product to a strained β-lactone during release from the NRPS assembly line.

Jason E Schaffer
Margaret R Reck
Timothy A Wencewicz
Research15 May 2017
Nature Chemical Biology

Volume: 13, P: 737-744
Publisher Correction: Structure of anhydrotetracycline-bound Tet(X6) reveals the mechanism for inhibition of type 1 tetracycline destructases

Hirdesh Kumar
Emily E. Williford
Niraj H. Tolia
Amendments and CorrectionsOpen Access11 May 2023
Communications Biology

Volume: 6, P: 1
Sequence-structure-function characterization of the emerging tetracycline destructase family of antibiotic resistance enzymes

Deep investigation of the sequence-structure-function landscape of the tetracycline destructase family of antibiotic resistance enzymes identifies new enzymes, and amino acid spositions essential to activity.

Kevin S. Blake
Hirdesh Kumar
Gautam Dantas
ResearchOpen Access16 Mar 2024
Communications Biology

Volume: 7, P: 1-16
Structure of anhydrotetracycline-bound Tet(X6) reveals the mechanism for inhibition of type 1 tetracycline destructases

Structural and biochemical characterization reveals that anhydrotetracycline’s mode of binding and inhibition of type 1 tetracycline destructases (TDases) is distinct from type 2 TDases.

Hirdesh Kumar
Emily E. Williford
Niraj H. Tolia
ResearchOpen Access17 Apr 2023
Communications Biology

Volume: 6, P: 1-10
Tetracycline-inactivating enzymes from environmental, human commensal, and pathogenic bacteria cause broad-spectrum tetracycline resistance

Gasparrini et al. show that Tet(X7) contributes to tetracycline resistance in a clinical Pseudomonas aeruginosa isolate and demonstrate the use of a Tet(X) inhibitor to circumvent resistance. This study highlights the importance of tet(X)-mediated antibiotic resistance and inhibition-based strategies for countering it.

Andrew J. Gasparrini
Jana L. Markley
Gautam Dantas
ResearchOpen Access15 May 2020
Communications Biology

Volume: 3, P: 1-12
Prospects for new antibiotics: a molecule-centered perspective

Christopher T Walsh
Timothy A Wencewicz
Reviews12 Jun 2013
The Journal of Antibiotics

Volume: 67, P: 7-22

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