Peptidoglycan from Akkermansia muciniphila MucT: chemical structure and immunostimulatory properties of muropeptides

Pilar Garcia-Vello*, Hanne L.P. Tytgat, Joe Gray, Janneke Elzinga, Flaviana Di Lorenzo, Jacob Biboy, Daniela Vollmer, Cristina De Castro, Waldemar Vollmer, Willem M. De Vos, Antonio Molinaro

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Akkermansia muciniphila is an intestinal symbiont known to improve the gut barrier function in mice and humans. Various cell envelope components have been identified to play a critical role in the immune signaling of A. muciniphila, but the chemical composition and role of peptidoglycan (PG) remained elusive. Here, we isolated PG fragments from A. muciniphila MucT (ATCC BAA-835), analyzed their composition and evaluated their immune signaling capacity. Structurally, the PG of A. muciniphila was found to be noteworthy due of the presence of some nonacetylated glucosamine residues, which presumably stems from deacetylation of N-acetylglucosamine. Some of the N-acetylmuramic acid (MurNAc) subunits were O-acetylated. The immunological assays revealed that muropeptides released from the A. muciniphila PG could both activate the intracellular NOD1 and NOD2 receptors to a comparable extent as muropeptides from Escherichia coli BW25113. These data challenge the hypothesis that non-N-acetylattion of PG can be used as a NOD-1 evasion mechanism. Our results provide new insights into the diversity of cell envelope structures of key gut microbiota members and their role in steering host-microbiome interactions.

Original languageEnglish
Pages (from-to)712-719
Number of pages8
JournalGlycobiology
Volume32
Issue number8
DOIs
Publication statusPublished - 1 Aug 2022

Keywords

  • Akkermansia
  • Gram-negative bacteria
  • immunochemistry
  • microbiome
  • peptidoglycan

Fingerprint

Dive into the research topics of 'Peptidoglycan from Akkermansia muciniphila MucT: chemical structure and immunostimulatory properties of muropeptides'. Together they form a unique fingerprint.

Cite this