Peptidoglycan from Akkermansia muciniphila MucT: chemical structure and immunostimulatory properties of muropeptides
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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Peptidoglycan from Akkermansia muciniphila MucT: chemical structure and immunostimulatory properties of muropeptides. / Garcia-Vello, Pilar; Tytgat, Hanne L P; Gray, Joe; Elzinga, Janneke; Lorenzo, Flaviana Di; Biboy, Jacob; Vollmer, Daniela; Castro, Cristina De; Vollmer, Waldemar; Vos, Willem M de; Molinaro, Antonio.
I: Glycobiology, Bind 32, Nr. 8, 2022, s. 712–719.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Peptidoglycan from Akkermansia muciniphila MucT: chemical structure and immunostimulatory properties of muropeptides
AU - Garcia-Vello, Pilar
AU - Tytgat, Hanne L P
AU - Gray, Joe
AU - Elzinga, Janneke
AU - Lorenzo, Flaviana Di
AU - Biboy, Jacob
AU - Vollmer, Daniela
AU - Castro, Cristina De
AU - Vollmer, Waldemar
AU - Vos, Willem M de
AU - Molinaro, Antonio
PY - 2022
Y1 - 2022
N2 - 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.
AB - 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.
U2 - 10.1093/glycob/cwac027
DO - 10.1093/glycob/cwac027
M3 - Journal article
C2 - 35452117
VL - 32
SP - 712
EP - 719
JO - Glycobiology
JF - Glycobiology
SN - 0959-6658
IS - 8
ER -
ID: 359858130