A family of di-glutamate mucin-degrading enzymes that bridges glycan hydrolases and peptidases

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

A family of di-glutamate mucin-degrading enzymes that bridges glycan hydrolases and peptidases. / Narimatsu, Yoshiki; Büll, Christian; Taleb, Víctor; Liao, Qinghua; Compañón, Ismael; Sánchez-Navarro, David; Durbesson, Fabien; Vincentelli, Renaud; Hansen, Lars; Corzana, Francisco; Rovira, Carme; Henrissat, Bernard; Clausen, Henrik; Joshi, Hiren J.; Hurtado-Guerrero, Ramon.

I: Nature Catalysis, Bind 7, 2024, s. 386–400.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Narimatsu, Y, Büll, C, Taleb, V, Liao, Q, Compañón, I, Sánchez-Navarro, D, Durbesson, F, Vincentelli, R, Hansen, L, Corzana, F, Rovira, C, Henrissat, B, Clausen, H, Joshi, HJ & Hurtado-Guerrero, R 2024, 'A family of di-glutamate mucin-degrading enzymes that bridges glycan hydrolases and peptidases', Nature Catalysis, bind 7, s. 386–400. https://doi.org/10.1038/s41929-024-01116-5

APA

Narimatsu, Y., Büll, C., Taleb, V., Liao, Q., Compañón, I., Sánchez-Navarro, D., Durbesson, F., Vincentelli, R., Hansen, L., Corzana, F., Rovira, C., Henrissat, B., Clausen, H., Joshi, H. J., & Hurtado-Guerrero, R. (2024). A family of di-glutamate mucin-degrading enzymes that bridges glycan hydrolases and peptidases. Nature Catalysis, 7, 386–400. https://doi.org/10.1038/s41929-024-01116-5

Vancouver

Narimatsu Y, Büll C, Taleb V, Liao Q, Compañón I, Sánchez-Navarro D o.a. A family of di-glutamate mucin-degrading enzymes that bridges glycan hydrolases and peptidases. Nature Catalysis. 2024;7:386–400. https://doi.org/10.1038/s41929-024-01116-5

Author

Narimatsu, Yoshiki ; Büll, Christian ; Taleb, Víctor ; Liao, Qinghua ; Compañón, Ismael ; Sánchez-Navarro, David ; Durbesson, Fabien ; Vincentelli, Renaud ; Hansen, Lars ; Corzana, Francisco ; Rovira, Carme ; Henrissat, Bernard ; Clausen, Henrik ; Joshi, Hiren J. ; Hurtado-Guerrero, Ramon. / A family of di-glutamate mucin-degrading enzymes that bridges glycan hydrolases and peptidases. I: Nature Catalysis. 2024 ; Bind 7. s. 386–400.

Bibtex

@article{dc6469cde10542f4a28383879aefc06b,

title = "A family of di-glutamate mucin-degrading enzymes that bridges glycan hydrolases and peptidases",

abstract = "Microbes utilize polysaccharides to protect their surfaces and build biofilms, whereas metazoans employ large mucins densely decorated with O-glycans to protect surfaces and keep microbes at a distance. However, gut microbes in mucus also feed on host mucins, thus imposing a need for continuous renewal to maintain protection, clearance and mucus homeostasis. Glycopeptidases that can cleave mucins are known, but mucinases that specifically cleave mucins are not. Here we report the discovery of such microbial mucinases that cleave mucins with trimmed glycans, recognize dense clusters of O-glycans, and employ a structural fold and catalytic machinery reminiscent of glycan hydrolases and peptidases. These di-glutamate mucinases are also found in eukaryotes, and we propose that they are designed to clear mucins following scavenging of O-glycans to promote healthy gut–microbiome homeostasis. (Figure presented.)",

author = "Yoshiki Narimatsu and Christian B{\"u}ll and V{\'i}ctor Taleb and Qinghua Liao and Ismael Compa{\~n}{\'o}n and David S{\'a}nchez-Navarro and Fabien Durbesson and Renaud Vincentelli and Lars Hansen and Francisco Corzana and Carme Rovira and Bernard Henrissat and Henrik Clausen and Joshi, {Hiren J.} and Ramon Hurtado-Guerrero",

note = "Publisher Copyright: {\textcopyright} The Author(s), under exclusive licence to Springer Nature Limited 2024.",

year = "2024",

doi = "10.1038/s41929-024-01116-5",

language = "English",

volume = "7",

pages = "386–400",

journal = "Nature Catalysis",

issn = "2520-1158",

publisher = "Macmillan Press",

}

RIS

TY - JOUR

T1 - A family of di-glutamate mucin-degrading enzymes that bridges glycan hydrolases and peptidases

AU - Narimatsu, Yoshiki

AU - Büll, Christian

AU - Taleb, Víctor

AU - Liao, Qinghua

AU - Compañón, Ismael

AU - Sánchez-Navarro, David

AU - Durbesson, Fabien

AU - Vincentelli, Renaud

AU - Hansen, Lars

AU - Corzana, Francisco

AU - Rovira, Carme

AU - Henrissat, Bernard

AU - Clausen, Henrik

AU - Joshi, Hiren J.

AU - Hurtado-Guerrero, Ramon

PY - 2024

Y1 - 2024

N2 - Microbes utilize polysaccharides to protect their surfaces and build biofilms, whereas metazoans employ large mucins densely decorated with O-glycans to protect surfaces and keep microbes at a distance. However, gut microbes in mucus also feed on host mucins, thus imposing a need for continuous renewal to maintain protection, clearance and mucus homeostasis. Glycopeptidases that can cleave mucins are known, but mucinases that specifically cleave mucins are not. Here we report the discovery of such microbial mucinases that cleave mucins with trimmed glycans, recognize dense clusters of O-glycans, and employ a structural fold and catalytic machinery reminiscent of glycan hydrolases and peptidases. These di-glutamate mucinases are also found in eukaryotes, and we propose that they are designed to clear mucins following scavenging of O-glycans to promote healthy gut–microbiome homeostasis. (Figure presented.)

AB - Microbes utilize polysaccharides to protect their surfaces and build biofilms, whereas metazoans employ large mucins densely decorated with O-glycans to protect surfaces and keep microbes at a distance. However, gut microbes in mucus also feed on host mucins, thus imposing a need for continuous renewal to maintain protection, clearance and mucus homeostasis. Glycopeptidases that can cleave mucins are known, but mucinases that specifically cleave mucins are not. Here we report the discovery of such microbial mucinases that cleave mucins with trimmed glycans, recognize dense clusters of O-glycans, and employ a structural fold and catalytic machinery reminiscent of glycan hydrolases and peptidases. These di-glutamate mucinases are also found in eukaryotes, and we propose that they are designed to clear mucins following scavenging of O-glycans to promote healthy gut–microbiome homeostasis. (Figure presented.)

U2 - 10.1038/s41929-024-01116-5

DO - 10.1038/s41929-024-01116-5

M3 - Journal article

AN - SCOPUS:85187289072

VL - 7

SP - 386

EP - 400

JO - Nature Catalysis

JF - Nature Catalysis

SN - 2520-1158

ER -

ID: 385692754