Propionibacterium freudenreichii
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA352469 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR4920034_1.fastq.gz | Fastqsanger.gz | |||
| SRR4920034_2.fastq.gz | Fastqsanger.gz | |||
| SRR4920035_1.fastq.gz | Fastqsanger.gz | |||
| SRR4920035_2.fastq.gz | Fastqsanger.gz | |||
| SRR4920036_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 12 |
Similar Datasets
Project description:Histone lysine lactylation (Klac) is a new posttranslational modification (PTM) that is installed by acetyltransferase to modulate specific immune responses1 and oncogenesis2,3. Akkermansia muciniphila (A. muciniphila) is a beneficial bacterium that blunts ulcerative colitis (UC) in a mouse model by secreting extracellular vesicles (SEVs)4. Although many histone sites are known to contain lysine lactylation, whether this modification is regulated to modulate specific biological functions by exogenous acetyltransferase or intestinal microbiota is not well understood. Here, we discovered that SEV from A. muciniphila, rather than A. muciniphila per se, has anti-Th17 (T helper 17) differentiation activity. We further screened the composition of SEV and found that Amuc_2172 is the key active component. As a GCN5-related acetyltransferase of A. muciniphila, Amuc_2172 is accessible to naïve T cells and functions as a lactylation transferase on Lys4 of histone H3. Accelerated histone H3 lactylation (H3Klac) on Lys4 competitively blocks trimethylation (H3Kme3) on Il17a loci in the process of Th17-cell differentiation. Additionally, intraperitoneal application of recombinant Amuc_2172 also inhibited Th17 and dextran sulfate sodium (DSS)-induced UC phenotypes in vivo; moreover, bioengineered Amuc_2172 showed improved colitis site delivery and higher Th17 inhibition potential compared to Amuc_2172 alone. Our study reveals not only a potential therapeutic strategy for treating colitis but also a model via which lysine lactylation is regulated by the intestinal microbiota, which may be broadly applicable to understand the crosstalk of bacteria and immunity.
2023-11-28 | PXD037100 | Pride
Project description:Histone lysine lactylation (Klac) is a new posttranslational modification (PTM) that is installed by acetyltransferase to modulate specific immune responses1 and oncogenesis2,3. Akkermansia muciniphila (A. muciniphila) is a beneficial bacterium that blunts ulcerative colitis (UC) in a mouse model by secreting extracellular vesicles (SEVs)4. Although many histone sites are known to contain lysine lactylation, whether this modification is regulated to modulate specific biological functions by exogenous acetyltransferase or intestinal microbiota is not well understood. Here, we discovered that SEV from A. muciniphila, rather than A. muciniphila per se, has anti-Th17 (T helper 17) differentiation activity. We further screened the composition of SEV and found that Amuc_2172 is the key active component. As a GCN5-related acetyltransferase of A. muciniphila, Amuc_2172 is accessible to naïve T cells and functions as a lactylation transferase on Lys4 of histone H3. Accelerated histone H3 lactylation (H3Klac) on Lys4 competitively blocks trimethylation (H3Kme3) on Il17a loci in the process of Th17-cell differentiation. Additionally, intraperitoneal application of recombinant Amuc_2172 also inhibited Th17 and dextran sulfate sodium (DSS)-induced UC phenotypes in vivo; moreover, bioengineered Amuc_2172 showed improved colitis site delivery and higher Th17 inhibition potential compared to Amuc_2172 alone. Our study reveals not only a potential therapeutic strategy for treating colitis but also a model via which lysine lactylation is regulated by the intestinal microbiota, which may be broadly applicable to understand the crosstalk of bacteria and immunity.
2023-11-29 | PXD037142 | Pride
Project description:Propionibacterium freudenreichii overview
| PRJNA35885 | ENA
Project description:Adaptation of Propionibacterium freudenreichii to the colon environment
| PRJNA215993 | ENA
Project description:Propionibacterium freudenreichii MJ2 Genome sequencing and assembly
| PRJNA918783 | ENA
Project description:Adaptation of Propionibacterium freudenreichii to long-term survival under gradual nutritional shortage
| PRJNA304515 | ENA
Project description:Transcriptome profiling of Propionibacterium freudenreichii strains associated with different anti-inflammatory properties.
| PRJNA345221 | ENA
Project description:Propionibacterium freudenreichii is used as a ripening culture in Swiss cheese manufacture. It produces flavor compounds over the whole ripening period. During cheese ripening, P. freudenreichii is exposed to a temperature downshift, especially when cheeses are transferred from warm temperature (about 24°C) to cold temperature (about 4°C). The aim of this study was to investigate the adaptation of P. freudenreichii at cold temperature by means of the first global gene expression profile for this species. The temporal transcriptomic response of P. freudenreichii was analyzed at five times of growth, during growth at 30°C then for 9 days at 4°C, in the constant presence of lactate as the main carbon source. P. freudenreichii response was also investigated by RT-qPCR for 30 genes, by proteomics and metabolomics (main metabolites quantified in culture supernatant). Microarray analysis revealed that 565 genes (25% of the protein-coding sequences of P. freudenreichii genome) were differentially expressed during transition from warm to cold temperature (P < 0.05 and |fold change| > 1). Most of the down-expressed genes were involved in cell machinery (cell division, protein turnover, translation, transcription and DNA replication). During incubation at cold temperature, P. freudenreichii accumulated carbon supplies by up-regulating genes involved in lactate, alanine and serine conversion to pyruvate, in gluconeogenesis and in glycogen synthesis. Interestingly, some genes involved in the formation of important flavor compounds of cheese, coding for an extracellular lipolytic esterases and enzymes of the pathways of formation of branched-chain compounds, were not significantly affected by cold. In conclusion, P. freudenreichii is metabolically active at cold temperature and induces pathways to maintain its long-term viability, which could explain its contribution to cheese ripening even at low temperature.
2011-12-01 | GSE30841 | GEO
Project description:PFEVs inhibit osteoclast differentiation by interfering RANK-RANKL binding, thereby decreasing expression of gene related to osteoclast differentiation and improve CIA, probably through inhibiting inflammation and osteoclastogenesis.
2024-11-04 | PXD051291 | Pride
Project description:Heterologous bacteriocin production in Propionibacterium freudenreichii is described. We developed an efficient system for DNA shuttling between Escherichia coli and P. freudenreichii using vector pAMT1. It is based on the P. freudenreichii rolling-circle replicating plasmid pLME108 and carries the cml(A)/cmx(A) chloramphenicol resistance marker. Introduction of the propionicin T1 structural gene (pctA) into pAMT1 under the control of the constitutive promoter (P4) yielded bacteriocin in amounts equal to those of the wild-type producer Propionibacterium thoenii 419. The P. freudenreichii clone showed propionicin T1 activity in coculture, killing 90% of sensitive bacteria within 48 h. The pamA gene from P. thoenii 419 encoding the protease-activated antimicrobial peptide (PAMP) was cloned and expressed in P. freudenreichii, resulting in secretion of the pro-PAMP protein. Like in the wild type, PAMP activation was dependent on externally added protease. Secretion of the antimicrobial peptide was obtained from a clone in which the pamA signal peptide and PAMP were fused in frame. The promoter region of pamA was identified by fusion of putative promoter fragments to the coding sequence of the pctA gene. The P4 and Ppamp promoters directed constitutive gene expression, and activity of both promoters was enhanced by elements upstream of the promoter core region.
| S-EPMC1317351 | biostudies-literature