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Bacteria like sharing their sweets.

Jon Cuccui1, Brendan W Wren

  • 1Department of Pathogen Molecular Biology, The London School of Hygiene and Tropical Medicine, London, WC1E 7HT, UK.

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Acinetobacter baumannii uses the same sugar building blocks for both protein glycosylation and capsule synthesis. Disrupting this shared pathway, essential for virulence and biofilm formation, offers a novel antimicrobial target.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Pathogenesis

Background:

  • Protein glycosylation and capsular polysaccharide formation are crucial for bacterial pathogen survival and virulence.
  • Acinetobacter baumannii is an opportunistic pathogen where these processes are critical.

Purpose of the Study:

  • To investigate the biosynthesis of a pentasaccharide in Acinetobacter baumannii 17978.
  • To understand the relationship between glycoprotein decoration and capsule biosynthesis.
  • To evaluate the role of these pathways in biofilm formation and pathogenesis.

Main Methods:

  • Structural analysis of Acinetobacter baumannii 17978.
  • Disruption of the PglC glycosyltransferase.
  • Assessment of biofilm formation and pathogenesis.

Main Results:

  • A pentasaccharide decorating glycoproteins shares building blocks with capsule biosynthesis.
  • Disruption of PglC abolished both glycoprotein production and capsule biosynthesis.
  • Both pathways are vital for biofilm formation and pathogenesis in Acinetobacter baumannii.

Conclusions:

  • Acinetobacter baumannii employs a shared glycan biosynthesis pathway for both protein glycosylation and capsule formation.
  • This shared pathway is essential for virulence and biofilm development.
  • Targeting this shared pathway presents a promising strategy for antimicrobial drug design.