Prospecting for microbial α-N-acetylgalactosaminidases yields a new class of GH31 O-glycanase

Rahfeld, Peter; Wardman, Jacob F.; Mehr, Kevin; Huff, Drew; Morgan-Lang, Connor; Chen, Hongming; Hallam, Steven J.; Withers, Stephen G.

doi:10.1074/jbc.ra119.010628

Cited by 27 publications

(17 citation statements)

References 80 publications

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“…The hydrolytic activities of both MBP‐BmNag31 and BmGH31 were tested against various para ‐nitrophenyl (pNP) glycosides. The enzymes hydrolyzed p‐ nitrophenyl N ‐acetyl‐α‐D‐galactosaminide (GalNAcα‐pNP) but not GlcNAc‐β‐1,3‐GalNAcα‐pNP and the other substrate, indicating that BmNag31 is an exo‐acting αGalNAcase, which matches the activity of its bacterial homologs (Cao et al ., 2020; Rahfeld et al ., 2019). In addition, BmGH31 was active towards bovine submaxillary mucin (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The Nag31s (BcGH31 and BpGH31) in bacteria isolated from human feces work with other carbohydrate‐active enzymes in cleaving peptide‐linked GalNAc for uptake (Rahfeld et al ., 2019). The lumen of the mammalian intestine is covered by a highly developed mucosal layer that is mainly composed of mucins, ie, heterologous O ‐GalNAc glycans attached to proteins (Bergstrom and Xia, 2013).…”

Section: Discussionmentioning

confidence: 99%

“…A recent report indicates that the GH31 proteins, BpGH31 and BcGH31, from the human gut bacteria Phocaeicola plebeius (formerly Bacteroides plebeius ) and Bacteroides caccae , respectively, exhibit α‐ N ‐acetylgalactosaminidase (αGalNAcase) activity, removing the O ‐linked α‐ N ‐acetylgalactosamine (GalNAc) residue from a glycopeptide but not the blood type A antigen (Rahfeld et al ., 2019). Moreover, we recently determined the crystal structure of GH31 αGalNAcase (EfNag31A) from E. faecalis (Miyazaki and Park, 2020).…”

Section: Introductionmentioning

confidence: 99%

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Biochemical characterization of Bombyx mori α‐N‐acetylgalactosaminidase belonging to the glycoside hydrolase family 31

Ikegaya

Miyazaki

Park

2021

Insect Molecular Biology

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Horizontal gene transfer is an important evolutionary mechanism not only for bacteria but also for eukaryotes. In the domestic silkworm Bombyx mori, a model species of lepidopteran insects, some enzymes are known to have been acquired by horizontal transfer; however, the enzymatic features of protein BmNag31, belonging to glycoside hydrolase family 31 (GH31) and whose gene was predicted to be transferred from Enterococcus sp. are unknown. In this study, we reveal that the transcription of BmNag31 increases significantly during the prepupal to pupal stage, and decreases in the adult stage. The full‐length BmNag31 and its truncated mutants were heterologously expressed in Escherichia coli and characterized. Its catalytic domain exhibits α‐N‐acetylgalactosaminidase activity and the carbohydrate‐binding module family 32 domain shows binding activity towards N‐acetylgalactosamine, similar to the Enterococcus faecalis homolog, EfNag31A. Gel filtration chromatography and blue native polyacrylamide gel electrophoresis analyses indicate that BmNag31 forms a hexamer whereas EfNag31A is monomeric. These results provide insights into the function of lepidopteran GH31 α‐N‐acetylgalactosaminidase.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Biochemical characterization of Bombyx mori α‐N‐acetylgalactosaminidase belonging to the glycoside hydrolase family 31

Ikegaya

Miyazaki

Park

2021

Insect Molecular Biology

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“…2019 ). In addition, a high throughput screening approach led to the identification of novel GH31 and GH109 enzymes with α-GalNAcase activity ( Rahfeld et al. 2019 ).…”

Section: Mucin Glycan Degradation Strategies By Gut Commensal Bacteriamentioning

confidence: 99%

“…The α-GalNAcase GH31 enzymes act solely upon the GalNAc present in core structures of mucin-type O -glycans with no activity toward blood type A-antigens. The putative PULs in which the described α-GalNAcase GH31 enzymes are located showed no similarity to known mucin-degrading PULs ( Rahfeld et al. 2019 ).…”

Section: Mucin Glycan Degradation Strategies By Gut Commensal Bacteriamentioning

confidence: 99%

Mucosal glycan degradation of the host by the gut microbiota

Bell

Juge

2020

Glycobiology

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The gut microbiota plays a major role in human health and an alteration in gut microbiota structure and function has been implicated in several diseases. In the colon, mucus covering the epithelium is critical to maintain a homeostatic relationship with the gut microbiota by harbouring a microbial community at safe distance from the epithelium surface. The mucin glycans composing the mucus layer provide binding sites and a sustainable source of nutrients to the bacteria inhabiting the mucus niche. Access to these glycan chains require a complement of glycoside hydrolases (GHs) produced by bacteria across the phyla constituting the human gut microbiota. Due to the increased recognition of the role of mucus-associated microbes in human health, how commensal bacteria breakdown and utilise host mucin glycans has become of increased interest and is reviewed here. This short review provides an overview of the strategies evolved by gut commensal bacteria to access this rich source of nutrient with a focus on the GHs involved in mucin degradation.

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Crystal structure of the Enterococcus faecalis α‐N‐acetylgalactosaminidase, a member of the glycoside hydrolase family 31

Miyazaki

Park

2020

FEBS Letters

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Prospecting for microbial α-N-acetylgalactosaminidases yields a new class of GH31 O-glycanase

Cited by 27 publications

References 80 publications

Biochemical characterization of Bombyx mori α‐N‐acetylgalactosaminidase belonging to the glycoside hydrolase family 31

Biochemical characterization of Bombyx mori α‐N‐acetylgalactosaminidase belonging to the glycoside hydrolase family 31

Mucosal glycan degradation of the host by the gut microbiota

Crystal structure of the Enterococcus faecalis α‐N‐acetylgalactosaminidase, a member of the glycoside hydrolase family 31

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