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Human gut microbes express functionally distinct endoglycosidases to metabolize the same N-glycan substrate
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Human gut microbes express functionally distinct endoglycosidases to metabolize the same N-glycan substrate
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Journal Article
Human gut microbes express functionally distinct endoglycosidases to metabolize the same N-glycan substrate
2024
Overview
Bacteroidales (syn. Bacteroidetes) are prominent members of the human gastrointestinal ecosystem mainly due to their efficient glycan-degrading machinery, organized into gene clusters known as polysaccharide utilization loci (PULs). A single PUL was reported for catabolism of high-mannose (HM)
N
-glycan glyco-polypeptides in the gut symbiont
Bacteroides thetaiotaomicron
, encoding a surface endo-β-N-acetylglucosaminidase (ENGase), BT3987. Here, we discover an ENGase from the GH18 family in
B. thetaiotaomicron
, BT1285, encoded in a distinct PUL with its own repertoire of proteins for catabolism of the same HM
N
-glycan substrate as that of BT3987. We employ X-ray crystallography, electron microscopy, mass spectrometry-based activity measurements, alanine scanning mutagenesis and a broad range of biophysical methods to comprehensively define the molecular mechanism by which BT1285 recognizes and hydrolyzes HM
N
-glycans, revealing that the stabilities and activities of BT1285 and BT3987 were optimal in markedly different conditions. BT1285 exhibits significantly higher affinity and faster hydrolysis of poorly accessible HM
N
-glycans than does BT3987. We also find that two HM-processing endoglycosidases from the human gut-resident
Alistipes finegoldii
display condition-specific functional properties. Altogether, our data suggest that human gut microbes employ evolutionary strategies to express distinct ENGases in order to optimally metabolize the same
N-
glycan substrate in the gastroinstestinal tract.
The human gut microbiome has a substantial impact on human health. Here, the authors find that prominent human gut microbes express functionally distinct surface endo-β-N-acetylglucosaminidases encoded by different polysaccharide utilization loci to optimally metabolize the same oligomannose
N-
glycan substrate in the gastrointestinal tract.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 147/143
/ 82/103
/ 82/16
/ 82/29
/ 82/80
/ 82/83
/ Alanine
/ Bacteria
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Bacteroides thetaiotaomicron - enzymology
/ Bacteroides thetaiotaomicron - genetics
/ Bacteroides thetaiotaomicron - metabolism
/ Enzymes
/ Glycan
/ Glycoside Hydrolases - genetics
/ Glycoside Hydrolases - metabolism
/ Humanities and Social Sciences
/ Humans
/ Mannose
/ Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics
/ Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism
/ Polysaccharides - metabolism
/ Proteins
/ Science
