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Prevotella bryantii B14

ABSTRACT: Prevotella bryantii B14 genome sequencing project

PROVIDER: PRJNA47067 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ADWO01.dat.gz	Other
	ADWO01.fasta.gz	Fasta.gz
	ADWO01.master.dat	Other
	ADWO01.dat.gz	Other

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1 - 4 of 4

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Prevotella monensin concentration

Project description:Prevotella bryantii B14 was cultivated with monensin. Growth was monitored over a period of 9h with a broad range of monensin concentrations.

2021-10-13 | PXD026085 | Pride

Prevotella bryantii B14 isolate:DSM 11371

Project description:Prevotella bryantii DSM 11371 genome sequencing

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Prevotella bryantii B14 proteins from in vitro cultivation under various short-chain fatty acids (SCFA)

Project description:P. bryantii B14 cells were cultivated separately in acetic (Acet), propionic (Prop), butyric (But), iso-butyric (iBut), valeric (Val), iso-valeric (iVal) and 2-methyl butyric acid (2MB) as well as in a mixture of all mentioned short-chain fatty acids (Mix). All 8 treatments were analyzed regarding their proteomes in order to understand the requirements and effects of each SCFA on the metabolism.

2021-09-09 | PXD016407 | Pride

Prevotella bryantii

Project description:Prevotella bryantii overview

| PRJNA47093 | ENA

Prevotella bryantii C21a

Project description:Prevotella bryantii C21a

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Prevotella bryantii strain:KHPX14

Project description:Prevotella bryantii KHPX14 genome sequencing

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Prevotella bryantii strain:fb3001

Project description:Prevotella bryantii FB3001 genome sequencing

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Prevotella_monensin_time series

Project description:Prevotella bryantii B14 was cultivated with monensin. Growth was monitored over a period of 72h including frequent sampling of cells.

2021-10-13 | PXD026057 | Pride

Short-Chain Fatty Acids Modulate Metabolic Pathways and Membrane Lipids in Prevotella bryantii B14.

Project description:Short-chain fatty acids (SCFAs) are bacterial products that are known to be used as energy sources in eukaryotic hosts, whereas their role in the metabolism of intestinal microbes is rarely explored. In the present study, acetic, propionic, butyric, isobutyric, valeric, and isovaleric acid, respectively, were added to a newly defined medium containing Prevotella bryantii B14 cells. After 8 h and 24 h, optical density, pH and SCFA concentrations were measured. Long-chain fatty acid (LCFA) profiles of the bacterial cells were analyzed via gas chromatography-time of flight-mass spectrometry (GC-ToF MS) and proteins were quantified using a mass spectrometry-based, label-free approach. Cultures supplemented with single SCFAs revealed different growth behavior. Structural features of the respective SCFAs were identified in the LCFA profiles, which suggests incorporation into the bacterial membranes. The proteomes of cultures supplemented with acetic and valeric acid differed by an increased abundance of outer membrane proteins. The proteome of the isovaleric acid supplementation showed an increase of proteins in the amino acid metabolism. Our findings indicate a possible interaction between SCFAs, the lipid membrane composition, the abundance of outer membrane proteins, and a modulation of branched chain amino acid biosynthesis by isovaleric acid.

| S-EPMC7709123 | biostudies-literature

Functional diversity of four glycoside hydrolase family 3 enzymes from the rumen bacterium Prevotella bryantii B14.

Project description:Prevotella bryantii B(1)4 is a member of the phylum Bacteroidetes and contributes to the degradation of hemicellulose in the rumen. The genome of P. bryantii harbors four genes predicted to encode glycoside hydrolase (GH) family 3 (GH3) enzymes. To evaluate whether these genes encode enzymes with redundant biological functions, each gene was cloned and expressed in Escherichia coli. Biochemical analysis of the recombinant proteins revealed that the enzymes exhibit different substrate specificities. One gene encoded a cellodextrinase (CdxA), and three genes encoded beta-xylosidase enzymes (Xyl3A, Xyl3B, and Xyl3C) with different specificities for either para-nitrophenyl (pNP)-linked substrates or substituted xylooligosaccharides. To identify the amino acid residues that contribute to catalysis and substrate specificity within this family of enzymes, the roles of conserved residues (R177, K214, H215, M251, and D286) in Xyl3B were probed by site-directed mutagenesis. Each mutation led to a severely decreased catalytic efficiency without a change in the overall structure of the mutant enzymes. Through amino acid sequence alignments, an amino acid residue (E115) that, when mutated to aspartic acid, resulted in a 14-fold decrease in the k(cat)/K(m) for pNP-beta-d-xylopyranoside (pNPX) with a concurrent 1.1-fold increase in the k(cat)/K(m) for pNP-beta-d-glucopyranoside (pNPG) was identified. Amino acid residue E115 may therefore contribute to the discrimination between beta-xylosides and beta-glucosides. Our results demonstrate that each of the four GH3 enzymes has evolved to perform a specific role in lignopolysaccharide hydrolysis and provide insight into the role of active-site residues in catalysis and substrate specificity for GH3 enzymes.

| S-EPMC2863481 | biostudies-literature

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