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

Autor:	Garcia-Vello P; Department of Chemical Sciences, University of Naples Federico II, Napoli 80126, Italy., Tytgat HLP; Laboratory of Microbiology, Wageningen University, Wageningen 6708 WE, The Netherlands., Gray J; Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4AX, UK., Elzinga J; Laboratory of Microbiology, Wageningen University, Wageningen 6708 WE, The Netherlands., Di Lorenzo F; Department of Agricultural Sciences, University of Naples Federico II, Portici 80055, Italy., Biboy J; Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4AX, UK., Vollmer D; Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4AX, UK., De Castro C; Department of Agricultural Sciences, University of Naples Federico II, Portici 80055, Italy., Vollmer W; Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4AX, UK., de Vos WM; Laboratory of Microbiology, Wageningen University, Wageningen 6708 WE, The Netherlands.; Human Microbiome Research Program, Faculty of Medicine, University of Helsinki, Helsinki 00014, Finland., Molinaro A; Department of Chemical Sciences, University of Naples Federico II, Napoli 80126, Italy.; Department of Chemistry, School of Science, Osaka University, 560-0043, Japan.
Jazyk:	angličtina
Zdroj:	Glycobiology [Glycobiology] 2022 Jul 13; Vol. 32 (8), pp. 712-719.
DOI:	10.1093/glycob/cwac027
Abstrakt:	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. (© The Author(s) 2022. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.)
Databáze:	MEDLINE
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