RadA, a MSCRAMM Adhesin of the Dominant Symbiote Ruminococcus gnavus E1, Binds Human Immunoglobulins and Intestinal

Marc Maresca1, Radia Alatou2, Ange Pujol1

  • 1Aix Marseille University, CNRS, Centrale Marseille, ISM2, IM2B, 13007 Marseille, France.

Biomolecules
|November 27, 2021
PubMed

Insights

Ruminococcus gnavus E1 expresses RadA, a gut-colonizing adhesin, which binds human immunoglobulins and mucins. This adhesin targets specific galactose and N-acetyl-galactosamine motifs on host cells.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Gastroenterology

Background:

  • Bacterial adhesion to the digestive mucosa is crucial for gut colonization.
  • Ruminococcus gnavus is a gut bacterium whose adhesion mechanisms require further elucidation.

Purpose of the Study:

  • To investigate the role of the RadA adhesin from Ruminococcus gnavus E1 in gut mucosal adhesion.
  • To identify the specific molecular targets of the RadA adhesin.

Main Methods:

  • Analysis of radA gene expression during gut colonization.
  • Characterization of the RadA N-terminal region's binding properties using various substrates.
  • Competition assays with lectins and monosaccharides to identify binding motifs.

Main Results:

  • Ruminococcus gnavus E1 expresses the RadA adhesin specifically during gut colonization.
  • The RadA N-terminal region binds human immunoglobulins (IgA, IgG) and intestinal mucins.
  • RadA recognizes the protein backbone of IgG and glycan structures of mucins, specifically Galactose and N-Acetyl-Galactosamine motifs.

Conclusions:

  • RadA is an MSCRAMM family adhesin critical for Ruminococcus gnavus E1 gut persistence.
  • RadA mediates adhesion through interactions with host immunoglobulins and mucins via specific glycan recognition.

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