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Bacterial peptidoglycan binds to tubulin

R Dziarski1, M M Rasenick, D Gupta

  • 1Northwest Center for Medical Education, Indiana University School of Medicine, Gary, 46408, USA. rdziar@iunhaw1.iun.indiana.edu

Biochimica Et Biophysica Acta
|November 18, 2000
PubMed

Insights

Tubulin, a key cellular protein, binds strongly to peptidoglycan (PGN), a bacterial component. This interaction influences tubulin polymerization, impacting cellular responses to Gram-positive bacteria.

Area of Science:

  • Immunology
  • Cell Biology
  • Microbiology

Background:

  • Peptidoglycan (PGN) from Gram-positive bacteria activates macrophages via CD14 and TLR2.
  • Cellular binding proteins for PGN are crucial for understanding immune responses.

Purpose of the Study:

  • To identify cellular binding proteins for peptidoglycan (PGN) in macrophages.
  • To investigate the interaction between PGN and identified binding proteins, specifically tubulin.

Main Methods:

  • PGN-affinity chromatography and N-terminal micro-sequencing were employed.
  • Tubulin-PGN binding affinity and kinetics were characterized.
  • The effect of PGN and lipopolysaccharide (LPS) on tubulin polymerization was assessed.

Main Results:

  • Tubulin was identified as a major PGN-binding protein in mouse macrophages.
  • Tubulin-PGN binding demonstrated high affinity (100-150 nM) and specificity.
  • PGN modulated tubulin polymerization, with effects varying based on glycerol presence.

Conclusions:

  • Tubulin is a significant cellular receptor for peptidoglycan (PGN).
  • PGN binding influences tubulin polymerization dynamics, suggesting a novel role in macrophage activation and bacterial recognition.

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