The C-type lectin receptor MGL senses N-acetylgalactosamine on the unique Staphylococcus aureus ST395 wall teichoic

Malgorzata E Mnich1,2, Rob van Dalen1, David Gerlach3,4

  • 1Medical Microbiology, University Medical Center Utrecht, Utrecht University, Utrecht, The Netherlands.

Cellular Microbiology
|June 21, 2019
PubMed

Insights

Staphylococcus aureus uses unique wall teichoic acid modifications to interact with human immune receptors like MGL, influencing skin inflammation and pathogen clearance.

Area of Science:

  • Immunology
  • Microbiology
  • Dermatology

Background:

  • Staphylococcus aureus is a common skin bacterium causing infections.
  • Innate immune cells detect S. aureus via pattern-recognition receptors (PRRs).
  • Previous work identified langerin (CD207) recognizing N-acetylglucosamine on S. aureus WTA.

Purpose of the Study:

  • Investigate the interaction of S. aureus ST395 with human innate immune receptors.
  • Determine the role of TagN and GalNAc in this interaction.
  • Understand how this recognition impacts immune responses.

Main Methods:

  • Studied the binding of S. aureus ST395 to human Macrophage galactose-type lectin (MGL; CD301).
  • Utilized tagN gene deletion and heterologous expression in S. aureus.
  • Analyzed cytokine production by human dendritic cells upon encountering GalNAc-modified WTA.

Main Results:

  • S. aureus ST395 binds to MGL in a tagN- and GalNAc-dependent manner.
  • Heterologous expression of Staphylococcus lugdunensis tagN in S. aureus conferred MGL binding.
  • Detection of GalNAc on S. aureus ST395 WTA by dendritic cells enhanced cytokine production.

Conclusions:

  • S. aureus ST395 utilizes GalNAc-modified WTA for recognition by MGL.
  • This interaction is dependent on the TagN glycosyltransferase.
  • Differential recognition of S. aureus glycoprofiles by innate receptors influences immune responses and pathogen clearance.

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