Degradation of chondroitin sulfate A by a PUL-like operon in Tannerella forsythia

Nguyen, Peter Q.; Eshaque, Rony; Garland, Barbara Anne; Dang, Anthony; Suits, M.D.L.

doi:10.1371/journal.pone.0272904

Cited by 3 publications

(1 citation statement)

References 56 publications

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“…Other phylogenetically related microbes, such as Bacteroides thetaiotaomicron , have polysaccharide utilization loci (PUL) capable of scavenging host-derived saccharides when dietary polysaccharides are absent ( 54 ). T. forsythia contains a PUL-like operon, which may enhance its in vivo fitness during periodontitis development ( 55 ). Further studies will be required to fully elucidate the role of these microbial GUS enzymes and potential mutualism in the establishment of a dysbiotic microbiota.…”

Section: Discussionmentioning

confidence: 99%

Microbial β-glucuronidases drive human periodontal disease etiology

et al. 2023

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Periodontitis is a chronic inflammatory disease associated with persistent oral microbial dysbiosis. The human β-glucuronidase (GUS) degrades constituents of the periodontium and is used as a biomarker for periodontitis severity. However, the human microbiome also encodes GUS enzymes, and the role of these factors in periodontal disease is poorly understood. Here, we define the 53 unique GUSs in the human oral microbiome and examine diverse GUS orthologs from periodontitis-associated pathogens. Oral bacterial GUS enzymes are more efficient polysaccharide degraders and processers of biomarker substrates than the human enzyme, particularly at pHs associated with disease progression. Using a microbial GUS-selective inhibitor, we show that GUS activity is reduced in clinical samples obtained from individuals with untreated periodontitis and that the degree of inhibition correlates with disease severity. Together, these results establish oral GUS activity as a biomarker that captures both host and microbial contributions to periodontitis, facilitating more efficient clinical monitoring and treatment paradigms for this common inflammatory disease.

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Section: Discussionmentioning

confidence: 99%

Microbial β-glucuronidases drive human periodontal disease etiology

et al. 2023

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Identification and characterization of a PL35 GAGs lyase with 4-O-sulfated N-acetylgalactosamine (A-type)-rich structures producing property

Lu,

Wang,

et al. 2024

International Journal of Biological Macromolecules

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Comparative Genomics of Carbohydrate Utilization in Bacteria of the Family Sphaerochaetaceae: Evolutionary Origin of the Genes Encoding Galacturonidase and Unsaturated Rhamnogalacturonyl Hydrolase

Troshina,

Naumoff,

Rechkina

et al. 2024

Microbiology

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A comparative analysis of carbohydrate degradation proteins encoded in the currently available genomic sequences of bacteria of the family Sphaerochaetaceae, namely Sphaerochaeta associata GLS2T, S. globosa BuddyT, S. pleomorpha GrapesT, S. halotolerans 4-11T, S. halotolerans 585, Sphaerochaeta sp. S2, Sphaerochaeta sp. PS, and Parasphaerochaetacoccoides SPN1T was carried out. The genomes of Sphaerochaeta spp. encode a medium-sized and diverse set of proteins potentially involved in the degradation of different classes of carbohydrates, mainly oligosaccharides. All studied genomes encode glycoside hydrolases of the GH1, GH2, GH3, GH4, GH13, GH20, GH28, GH36, GH43, GH57, GH63, GH77 and GH105 families, as well as carbohydrate esterases of the CE8 and CE9 families. All studied bacteria, with the exception of P. coccoides SPN1T, have many genes of the GH31 family proteins. The studied members of Sphaerochaetaceae do not have genes coding for endo-β-acetylmuramidase (lysozyme) of the GH23 family, which participates in peptidoglycan turnover. However, the genomes of S. associata, S. globosa, Sphaerochaeta sp. PS, and S. pleomorpha contain exo-β-acetylmuramidase genes (GH171 family). A significant part of the genes encoding carbohydrate degradation enzymes have the closest homologues among representatives of the phyla Bacillota, Bacteroidota, and Pseudomonadota. The genomes of the studied bacteria encode proteins that could potentially be involved in the degradation of pectin. The ability of the Sphaerochaetaceae members to use pectin for growth, as well as the evolutionary origin of the genes encoding potential α-galacturonidase (GH4 family) and unsaturated glucuronyl/rhamnogalacturonyl hydrolase (GH105 family), which participate in the degradation of pectin components, were studied.

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Degradation of chondroitin sulfate A by a PUL-like operon in Tannerella forsythia

Cited by 3 publications

References 56 publications

Microbial β-glucuronidases drive human periodontal disease etiology

Microbial β-glucuronidases drive human periodontal disease etiology

Identification and characterization of a PL35 GAGs lyase with 4-O-sulfated N-acetylgalactosamine (A-type)-rich structures producing property

Comparative Genomics of Carbohydrate Utilization in Bacteria of the Family Sphaerochaetaceae: Evolutionary Origin of the Genes Encoding Galacturonidase and Unsaturated Rhamnogalacturonyl Hydrolase

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