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Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins
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Binding of Akkermansia muciniphila to mucin is O-glycan specific

Janneke Elzinga1,2, Yoshiki Narimatsu3,4, Noortje de Haan3,5

  • 1Laboratory of Microbiology, Wageningen University & Research, Wageningen, The Netherlands. jelzinga@sund.ku.dk.

Nature Communications
|May 29, 2024
PubMed

Insights

Akkermansia muciniphila binds to intestinal mucins by recognizing specific sugar structures. This binding is unaffected by oxygen or pasteurization, revealing key interactions for gut bacteria colonization.

Area of Science:

  • Microbiology
  • Glycobiology
  • Gastroenterology

Background:

  • Akkermansia muciniphila is an anaerobic gut bacterium that degrades mucins, essential for intestinal mucus.
  • Understanding A. muciniphila's mucin binding is crucial for its persistence and role as an intestinal symbiont.
  • Current knowledge on how A. muciniphila recognizes and adheres to mucins is limited.

Purpose of the Study:

  • To investigate the mucin-binding properties of A. muciniphila.
  • To identify specific O-glycan structures recognized by A. muciniphila.
  • To understand the role of bacterial enzymes in mucin binding.

Main Methods:

  • Assessing mucin-binding properties under varying oxygen concentrations and after pasteurization.
  • Utilizing a cell-based mucin array displaying human mucin tandem repeats with distinct O-glycans.
  • Analyzing the effect of A. muciniphila's endogenous neuraminidase activity on mucin binding.

Main Results:

  • A. muciniphila's mucin-binding ability is robust, independent of oxygen levels, and resistant to pasteurization.
  • The bacterium selectively recognizes the unsialylated N-acetyllactosamine (LacNAc) disaccharide on core2 and core3 O-glycans.
  • Endogenous A. muciniphila neuraminidase activity uncovers the LacNAc epitope, enhancing bacterial binding to mucins.

Conclusions:

  • A. muciniphila utilizes specific O-glycan recognition for mucin binding and colonization.
  • The bacterium's enzymatic activity plays a role in accessing and binding to its mucin substrate.
  • These findings provide critical insights into the colonization mechanisms of this important gut symbiont.

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