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Molecular basis of antibiotic self-resistance in a bee larvae pathogen

Tam Dang1, Bernhard Loll2, Sebastian Müller1

  • 1Institut für Chemie, Technische Universität Berlin, Berlin, Germany.

Nature Communications
|April 29, 2022
PubMed

Insights

The enzyme PamZ protects Paenibacillus larvae from its own antibiotic, paenilamicin, by acetylation. This mechanism is crucial for understanding the bacterium

Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • Paenibacillus larvae causes American Foulbrood, a severe honey bee disease.
  • The bacterium produces paenilamicin, a potent antibiotic with antibacterial and antifungal properties.
  • Paenilamicin's biosynthetic gene cluster includes the N-acetyltransferase gene, pamZ.

Purpose of the Study:

  • To investigate the function of PamZ in Paenibacillus larvae.
  • To elucidate the mechanism by which Paenibacillus larvae achieves self-resistance to paenilamicin.
  • To characterize the structural and biochemical properties of PamZ.

Main Methods:

  • Tandem mass spectrometry
  • Nuclear magnetic resonance spectroscopy
  • X-ray crystallography
  • Enzymatic assays

Main Results:

  • PamZ deactivates paenilamicin through N-acetylation of agmatinamic acid.
  • The crystal structure of PamZ:acetyl-CoA complex revealed a unique tandem-domain architecture.
  • A negatively-charged substrate-binding groove specifically binds cationic paenilamicin.
  • Identified the N-terminal amino group of agmatinamic acid as the N-acetylation site.

Conclusions:

  • PamZ functions as a self-resistance factor in Paenibacillus larvae.
  • Understanding PamZ-mediated deactivation is key to paenilamicin's role in pathogenicity.
  • Structural insights into PamZ aid in comprehending antibiotic resistance mechanisms.

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