Faecalibacterium duncaniae strain:A2165
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ABSTRACT:
PROVIDER: PRJNA394904 | ENA |
REPOSITORIES: ENA
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Project description:MAM (Microbial-Anti-Inflammatory Molecule) is a 14,5 kDa protein that is one of the best-known effector molecules with anti-inflammatory properties in Faecalibacterium duncaniae, a critical species in the human gut microbiota. Despite its importance, MAM function and molecular features remain poorly understood. Therefore, in this study, we sought to elucidate MAM's physiological importance. We investigated MAM localization using mass-spectrometry, immunogold labeling, and peptide secretion dynamics during bacterial growth. Bioinformatic analysis and microscopy further supported our understanding of MAM protein domain organization, interactions, and putative macromolecular assembly. Our results identified MAM as the most abundant protein in the cell envelope, and the second most abundant one in the overall proteome of F. duncaniae, with confirmed localization at the bacterial surface through immunogold labeling. Bioinformatics analysis highlights that MAM could comprise an N-terminal 21 residue leader peptide whose sequence contains all the motifs to be recognized and cleaved by a peptidase, followed by a 114 residue cargo peptide. Appropriately, in silico modeling suggests that the MAM leader peptide nicely accommodates the peptidase-domain-containing ABC transporter (PCAT) that is adjacent to MAM in the genome of F. duncaniae. After N-terminal excision, the cargo protein could be transported to the cell envelope via this PCAT, where it could assemble into a hexameric, pore-like structure, as revealed by AlphaFold3 modeling. Electron microscopy images of In situ F.duncaniae cells revealed a highly ordered lattice with repetitive units of hexamers. Moreover, an enriched fraction of MAM protein was obtained with in vitro LiCl extraction, exhibiting the same organizational pattern as the predicted hexameric organization. These findings provide the first comprehensive characterization and molecular export mechanisms of MAM as a key protein component of the F. duncaniae cell envelope, suggesting roles in cell structure, permeability, and communication with the host environment. It reveals a novel, lattice-like organization on the F. duncaniae cell envelope that may play a critical role in maintaining bacteria structure. This work introduces a novel discussion about the unique organization of the F.duncaniae cell envelope, having MAM as a key component for the bacteria, supporting the understanding of the unique biology of F. duncaniae and its potential as a next-generation probiotic or Live Biotherapeutics
2025-06-30 | PXD057939 | Pride
Project description:Faecalibacterium duncaniae A2-165 is a rod-shaped, non-motile, and Extremely Sensitive to Oxygen microorganism, belonging to one of the most abundant genera in the human gut microbiome. A decreased abundance of Faecalibacterium species is correlated to Inflammatory Bowel Diseases (IBDs), highlighting this genus as a marker of gut health and a promising Next-Generation Probiotic. Many studies have demonstrated the anti-inflammatory effect of the most studied species, F. duncaniae A2-165, on mouse models of IBDs, associating the disease amelioration and suppression of inflammatory markers with large amounts of butyrate produced by the bacteria, and the presence of the MAM protein. However, many factors in F. duncaniae metabolism could contribute to its importance in the gut. To address this issue, this study characterized the proteome of F. duncaniae A2-165 in the stationary phase through a LC-MS/MS label-free proteomics approach.We quantified 1.280 proteins in total, corresponding to 44,7% of the in silico predicted proteome, with clear distinction between insoluble and soluble protein abunndaces. The subcellular localization prediction of the quantified proteins revealed 802 cytoplasmic proteins, 265 membrane proteins, six extracellular proteins, eight cell wall proteins, and 199 unknown localization proteins. Differential abundance analysis between insoluble and soluble fraction showed 290 proteins more abundant and 330 less abundant in the insoluble fraction. Functional analysis of these proteins showed a predominance of transporter proteins in the insoluble fraction, while metabolism of amino acids, carbohydrates and nucleotides were predominant in the soluble fraction. Further analysis of enriched pathways for each fraction showed energy metabolism, carbon cycle, and amino acid metabolism enriched in the soluble, and ABC transporters, quorum sensing, and oxidative phosphorylation in the insoluble. Moreover, we could confirm the presence of proteins associated to the bacteria’s mechanism of action, notably the key butyrate production pathway ButCoAT, the MAM protein and the ABC transporter exporter, and shikimate pathway enzymes.
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