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Discovery of Inhibitors for Bacterial Arr Enzymes ADP-Ribosylating and Inactivating Rifamycin Antibiotics.

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Researchers identified novel inhibitors targeting bacterial ADP-ribosyltransferase (Arr) enzymes, which confer rifamycin antibiotic resistance. These inhibitors show promise for overcoming drug resistance, despite not yet sensitizing bacteria in growth assays.

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Area of Science:

  • Biochemistry
  • Microbiology
  • Drug Discovery

Background:

  • ADP-ribosylation is a modification targeting proteins and, uniquely, rifamycin antibiotics.
  • Bacterial ADP-ribosyltransferase (Arr) enzymes inactivate rifampicin, leading to antibiotic resistance.
  • Arr enzymes are prevalent in pathogenic bacteria and associated with mobile genetic elements.

Purpose of the Study:

  • To identify small-molecule inhibitors of bacterial Arr enzymes.
  • To explore the potential of inhibiting Arr enzymes to overcome rifamycin resistance.

Main Methods:

  • Developed a high-throughput assay to screen a library of human ADP-ribosyltransferase-targeted compounds.
  • Tested identified inhibitors against Arr enzymes from *Mycolicibacterium smegmatis*, *Pseudomonas aeruginosa*, *Stenotrophomonas maltophilia*, and *Mycobacteroides abscessus*.
  • Utilized X-ray crystallography to determine the structures of *M. smegmatis* and *P. aeruginosa* Arr enzymes, including a complex with a potent inhibitor.

Main Results:

  • Identified 15 inhibitors with IC50 values below 5 μM against four different Arr enzymes.
  • Observed selectivity of inhibitors, attributed to structural differences in the NAD+ binding pockets of Arr homologues.
  • Determined the crystal structure of *M. smegmatis* Arr enzyme complexed with its most potent inhibitor (IC50 = 1.3 μM).

Conclusions:

  • The study provides a collection of novel Arr enzyme inhibitors and structural insights into their binding.
  • Structural differences in Arr homologues explain observed inhibitor selectivity.
  • While inhibitors did not sensitize *M. smegmatis* to rifampicin in growth assays, they offer a foundation for developing new anti-resistance strategies.