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Crystal structure of the Propionibacterium acnes surface sialidase, a drug target for P. acnes-associated diseases

Angel C Y Yu1,2, Gesa Volkers1,2, Seino A K Jongkees3

  • 1Department of Biochemistry and Molecular Biology, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia V6T 1Z3, Canada.

Glycobiology
|November 18, 2021
PubMed

Insights

Propionibacterium acnes (P. acnes) is an opportunistic pathogen. Structural analysis of its sialidase enzyme provides a basis for developing new small-molecule drugs against P. acnes infections.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Propionibacterium acnes (P. acnes) is a skin bacterium, often opportunistic, linked to acne and other infections.
  • P. acnes virulence is supported by its genome and surface enzymes like sialidase.
  • A P. acnes sialidase vaccine shows potential in reducing organism-induced inflammation and cytotoxicity.

Purpose of the Study:

  • To determine the crystal structures of P. acnes sialidase.
  • To analyze the enzyme's complex with a transition-state mimic.
  • To provide a foundation for structure-based drug design against P. acnes.

Main Methods:

  • X-ray crystallography was used to obtain the structures.
  • Kinetic analyses were performed.
  • A glycan array screen was employed to probe enzyme specificities.

Main Results:

  • The crystal structures of P. acnes sialidase and its complex with Neu5Ac2en were determined.
  • Structural and kinetic data revealed specificities for α-2,3-sialosides.
  • These findings offer insights into enzyme function and inhibition.

Conclusions:

  • The determined structures provide a blueprint for designing novel therapeutics.
  • Structure-based design can yield small-molecule inhibitors targeting P. acnes sialidase.
  • This research paves the way for new treatments for P. acnes-associated diseases.
Keywords:
Propionibacterium acnesacne vulgarissialidase

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