PUL ID

PUL0663

PubMed

34340552, mBio. 2021 Aug 31;12(4):e0136821. doi: 10.1128/mBio.01368-21. Epub 2021 Aug 3.

Characterization method

thin layer chromatography,clone and expression,recombinant protein expression

Genomic accession number

NZ_DS990123.1

Nucelotide position range

30514-46197

Substrate

arabinogalactan protein

Loci

BACPLE_RS05590-BACPLE_RS05620

Species

Bacteroides plebeius DSM17135/310297

Degradation or Biosynthesis

degradation

Cluster number

1

Gene name

Gene position

Gene type

Found by CGCFinder?

- 1 - 2028 (-) CDS No
- 2045 - 5347 (-) TC: gnl|TC-DB|Q45780|1.B.14.6.1 Yes
- 5669 - 9697 (+) TF: DBD-Pfam|HTH_AraC,DBD-SUPERFAMILY|0035607 Yes
- 9768 - 10919 (-) CAZyme: GH43_24| GH43_24 Yes
- 10960 - 11952 (-) CAZyme: GH43_17| GH43_17 Yes
- 12082 - 13278 (-) CAZyme: GH105|GH154| GH154 Yes
- 14407 - 15684 (-) CAZyme: PL42|PL42 Yes

PUL ID

PUL0663

PubMed

34340552, mBio. 2021 Aug 31;12(4):e0136821. doi: 10.1128/mBio.01368-21. Epub 2021 Aug 3.

Title

Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius.

Author

Munoz-Munoz J, Ndeh D, Fernandez-Julia P, Walton G, Henrissat B, Gilbert HJ

Abstract

The human gut microbiota (HGM) contributes to the physiology and health of its host. The health benefits provided by dietary manipulation of the HGM require knowledge of how glycans, the major nutrients available to this ecosystem, are metabolized. Arabinogalactan proteins (AGPs) are a ubiquitous feature of plant polysaccharides available to the HGM. Although the galactan backbone and galactooligosaccharide side chains of AGPs are conserved, the decorations of these structures are highly variable. Here, we tested the hypothesis that these variations in arabinogalactan decoration provide a selection mechanism for specific Bacteroides species within the HGM. The data showed that only a single bacterium, B. plebeius, grew on red wine AGP (Wi-AGP) and seaweed AGP (SW-AGP) in mono- or mixed culture. Wi-AGP thus acts as a privileged nutrient for a Bacteroides species within the HGM that utilizes marine and terrestrial plant glycans. The B. plebeius polysaccharide utilization loci (PULs) upregulated by AGPs encoded a polysaccharide lyase, located in the enzyme family GH145, which hydrolyzed Rha-Glc linkages in Wi-AGP. Further analysis of GH145 identified an enzyme with two active sites that displayed glycoside hydrolase and lyase activities, respectively, which conferred substrate flexibility for different AGPs. The AGP-degrading apparatus of B. plebeius also contained a sulfatase, BpS1_8, active on SW-AGP and Wi-AGP, which played a pivotal role in the utilization of these glycans by the bacterium. BpS1_8 enabled other Bacteroides species to access the sulfated AGPs, providing a route to introducing privileged nutrient utilization into probiotic and commensal organisms that could improve human health. IMPORTANCE Dietary manipulation of the HGM requires knowledge of how glycans available to this ecosystem are metabolized. The variable structures that decorate the core component of plant AGPs may influence their utilization by specific organisms within the HGM. Here, we evaluated the ability of Bacteroides species to utilize a marine and terrestrial AGP. The data showed that a single bacterium, B. plebeius, grew on Wi-AGP and SW-AGP in mono- or mixed culture. Wi-AGP is thus a privileged nutrient for a Bacteroides species that utilizes marine and terrestrial plant glycans. A key component of the AGP-degrading apparatus of B. plebeius is a sulfatase that conferred the ability of the bacterium to utilize these glycans. The enzyme enabled other Bacteroides species to access the sulfated AGPs, providing a route to introducing privileged nutrient utilization into probiotic and commensal organisms that could improve human health.