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

doi:10.57711/wfha-fn22

Peptidoglycan from Akkermansia muciniphila Muc^T: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 journal › Article › Academic › peer-review

6 Citations (Scopus)

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 language	English
Pages (from-to)	712-719
Number of pages	8
Journal	Glycobiology
Volume	32
Issue number	8
DOIs	https://doi.org/10.57711/wfha-fn22 https://doi.org/10.1093/glycob/cwac027
Publication status	Published - 1 Aug 2022

Keywords

Akkermansia
Gram-negative bacteria
immunochemistry
microbiome
peptidoglycan

Access to Document

10.57711/wfha-fn22Licence: Open Access other
10.1093/glycob/cwac027

Cite this

Garcia-Vello, P., Tytgat, H. L. P., Gray, J., Elzinga, J., Di Lorenzo, F., Biboy, J., Vollmer, D., De Castro, C., Vollmer, W., De Vos, W. M., & Molinaro, A. (2022). Peptidoglycan from Akkermansia muciniphila Muc^T:chemical structure and immunostimulatory properties of muropeptides. Glycobiology, 32(8), 712-719. https://doi.org/10.57711/wfha-fn22, https://doi.org/10.1093/glycob/cwac027

@article{9c10b00556cf450dbf6e21a35df7df64,

title = "Peptidoglycan from Akkermansia muciniphila MucT: chemical structure and immunostimulatory properties of muropeptides",

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. ",

keywords = "Akkermansia, Gram-negative bacteria, immunochemistry, microbiome, peptidoglycan",

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

year = "2022",

month = aug,

day = "1",

doi = "10.57711/wfha-fn22",

language = "English",

volume = "32",

pages = "712--719",

journal = "Glycobiology",

issn = "0959-6658",

publisher = "Oxford University Press",

number = "8",

}

Garcia-Vello, P, Tytgat, HLP, Gray, J, Elzinga, J, Di Lorenzo, F, Biboy, J, Vollmer, D, De Castro, C, Vollmer, W, De Vos, WM & Molinaro, A 2022, 'Peptidoglycan from Akkermansia muciniphila Muc^T:chemical structure and immunostimulatory properties of muropeptides', Glycobiology, vol. 32, no. 8, pp. 712-719. https://doi.org/10.57711/wfha-fn22, https://doi.org/10.1093/glycob/cwac027

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 - Di Lorenzo, Flaviana

AU - Biboy, Jacob

AU - Vollmer, Daniela

AU - De Castro, Cristina

AU - Vollmer, Waldemar

AU - De Vos, Willem M.

AU - Molinaro, Antonio

PY - 2022/8/1

Y1 - 2022/8/1

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.

KW - Akkermansia

KW - Gram-negative bacteria

KW - immunochemistry

KW - microbiome

KW - peptidoglycan

U2 - 10.57711/wfha-fn22

DO - 10.57711/wfha-fn22

M3 - Article

C2 - 35452117

AN - SCOPUS:85134434094

SN - 0959-6658

VL - 32

SP - 712

EP - 719

JO - Glycobiology

JF - Glycobiology

IS - 8

ER -

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

Abstract

Keywords

Access to Document

Fingerprint

Cite this

Peptidoglycan from Akkermansia muciniphila Muc^T:chemical structure and immunostimulatory properties of muropeptides