Characterization of a Unique Carbohydrate-Binding Module from Akkermansia muciniphila that Binds Ganglioside-Associated Glycans
- 1Department of Biological Sciences, The University of Alabama, Tuscaloosa, Alabama 35487,United States
- 2Department of Biological Sciences, University of Calgary, Calgary T2N 1N4, Canada
Abstract
Akkermansia muciniphila is a mucin-degrading gut symbiont that promotes host metabolic health through its ability to utilize host-derived glycans. Central to this microbe is its diverse set of glycoside hydrolases (GHs), specifically GHs involved in degrading host glycans like mucin. Here, we characterize an A. muciniphila GH from family 123 (AmGH123), that has β-N-acetyl-d-galactosaminidase activity, removing terminal β-linked GalNAc from ganglioside-associated glycans similar to other GH123s. In addition, we identify and characterize a unique carbohydrate-binding module from family 32 associated with AmGH123 (AmGH123CBM32), representing the first CBM characterized from A. muciniphila. AmGH123CBM32 selectively binds GalNAc-terminated ganglioside-associated glycans, revealing previously unrecognized ligand specificity for CBM32 members. Structural analysis and site-directed mutagenesis reveal a distinct ligand-binding pocket in AmGH123CBM32, highlighting diverse strategies for glycan recognition within this family.
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BibTeX
@article{miller2026characterization,
title = {{Characterization of a Unique Carbohydrate-Binding Module from Akkermansia muciniphila that Binds Ganglioside-Associated Glycans}},
author = {Janique Miller and Joshua Steward and Davide Rossotto and Omid Haji-Ghassemi and Melanie A. Higgins},
journal = {Biochemistry},
year = {2026},
month = oct,
doi = {10.1021/acs.biochem.6c00509},
url = {https://doi.org/10.1021/acs.biochem.6c00509},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Characterization of a Unique Carbohydrate-Binding Module from Akkermansia muciniphila that Binds Ganglioside-Associated Glycans
AU - Janique Miller
AU - Joshua Steward
AU - Davide Rossotto
AU - Omid Haji-Ghassemi
AU - Melanie A. Higgins
PY - 2026
DA - 2026/10/15
JO - Biochemistry
DO - 10.1021/acs.biochem.6c00509
UR - https://doi.org/10.1021/acs.biochem.6c00509
AB - Akkermansia muciniphila is a mucin-degrading gut symbiont that promotes host metabolic health through its ability to utilize host-derived glycans. Central to this microbe is its diverse set of glycoside hydrolases (GHs), specifically GHs involved in degrading host glycans like mucin. Here, we characterize an A. muciniphila GH from family 123 (AmGH123), that has β-N-acetyl-d-galactosaminidase activity, removing terminal β-linked GalNAc from ganglioside-associated glycans similar to other GH123s. In addition, we identify and characterize a unique carbohydrate-binding module from family 32 associated with AmGH123 (AmGH123CBM32), representing the first CBM characterized from A. muciniphila. AmGH123CBM32 selectively binds GalNAc-terminated ganglioside-associated glycans, revealing previously unrecognized ligand specificity for CBM32 members. Structural analysis and site-directed mutagenesis reveal a distinct ligand-binding pocket in AmGH123CBM32, highlighting diverse strategies for glycan recognition within this family.
SN - 0006-2960
SN - 1520-4995
ER -