The phage-encoded PIT4 protein impacts the Pseudomonas aeruginosa type IV pili by affecting different two-component systems
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ABSTRACT:
PROVIDER: PRJNA962838 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR24333000_1.fastq.gz | Fastqsanger.gz | |||
| SRR24333000_2.fastq.gz | Fastqsanger.gz | |||
| SRR24333001_1.fastq.gz | Fastqsanger.gz | |||
| SRR24333001_2.fastq.gz | Fastqsanger.gz | |||
| SRR24333002_1.fastq.gz | Fastqsanger.gz |
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Project description:Two component systems (TCSs) control a large proportion of virulence factors in Pseudomonas aeruginosa. Yet, investigations on inhibitors of regulatory pathways of TCS remain scare, despite their potential in anti-virulence strategies. This work encompasses the working mechanism of PIT4, a protein derived from the lytic P. aeruginosa phage LSL4. This viral protein inhibits bacterial motility and in particular twitching motility, while reducing the virulence of P. aeruginosa towards HeLa cells. Via differential gene expression and a yeast two-hybrid screen, PIT4 was shown to interact with components of different two component systems. In one-on-one interaction assays, it was confirmed that PIT4 interacts with the histidine kinases FleS, PilS and PA2882, through interaction with the histidine kinase domain. As such, this work highlights the potential of previously unknown phage proteins in virulence regulation of multidrug resistant pathogens that might be exploited for anti-virulence strategies and biotechnological applications.
2023-09-25 | GSE230851 | GEO
Project description:Type IV pili (T4P) are prevalent, polymeric surface structures in pathogenic bacteria, making them ideal targets for effective vaccines. However, bacteria have evolved efficient strategies to evade type IV pili-directed antibody responses. Neisseria meningitidis are prototypical type IV pili-expressing Gram-negative bacteria responsible for life threatening sepsis and meningitis. This species has evolved several genetic strategies to modify the surface of its type IV pili based on recombination, phase variation and the presence of different alleles of genes involved in posttranslational modifications. This results in changes in pilin subunit amino acid sequence, nature of glycosylation and phosphoform modification, but how these different processes affect antibody binding at the structural level is still unknown. To explore this question, we provide cryo-electron microscopy structures of pili of different sequence types with sufficiently high resolution to visualize posttranslational modifications. We then generated nanobodies directed against type IV pili which alter pilus function in vitro and vivo; and determined their structures complexed with their pilus target. We also determined how the different types of pili surface modifications alter nanobody binding. These different structures shed light on the impressive complementarity between the different strategies used by bacteria to avoid antibody binding. Importantly, we also show that structural information can be used to make informed modifications in nanobodies as countermeasures to these immune evasion mechanisms.
2024-02-29 | PXD046119 | Pride
Project description:The phytopathogen Xylella fastidiosa produces two classes of pili, long type IV pili and short type I pili, which are involved in motility and adhesion. In this work, we have investigated the role of σ54 factor and its involvement in the regulation of fimbrial biogenesis in X. fastidiosa. An rpoN null mutant was constructed from citrus strain J1a12, and analyses of global gene expression profile by microarrays comparing the wild type and rpoN mutant strains showed that few genes exhibited differential expression. At least one gene, pilA1 (XF2542), which encodes the structural pilin protein of type IV fimbriae, showed decreased expression in the rpoN mutant whereas an operon encoding proteins of type I fimbriae were twofold more expressed in the mutant. Quantitative real time RT-PCR (qRT-PCR) analysis confirmed that pilA1 transcript was significantly reduced in the rpoN mutant. The transcriptional start site of pilA1 was determined by primer extension, and a canonical σ54-dependent promoter was found upstream of the start site. Genome sequence analysis of X. fastidiosa revealed five paralogues of pilA, but microarray and qRT-PCR data demonstrated that only the pilA1 transcript was significantly affected in the rpoN mutant. The rpoN mutant made more biofilm than the wild type strain and presented a cell-cell aggregative phenotype. These results indicate that σ54 regulates biofilm formation, probably via differential regulation of genes involved in type IV and type I fimbrial biogenesis. Keywords: rpoN mutant strain, pili
2007-10-22 | GSE8097 | GEO
Project description:Many bacteria express filaments called type IV pili on their surface, which are involved in motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Type IV pili are comprised of a helical assembly of repeating pilin subunits that allow both flexibility and strength. They are therefore powerful structures that enable bacterial proliferation and genetic adaptation, potentially leading to the development of pathogenicity and antibiotic resistance. They are also targets for drug development. By electron cryo-microscopy and mass spectrometry, we show that the bacterium Thermus thermophilus produces two forms of type IV pilus, differing in structure and protein composition. We have determined the structures of both and built atomic models, which reveal a new pilin, how the subunits assemble and their glycosylation patterns. We also delineate the roles of the two filaments in promoting twitching and natural transformation.
2020-03-09 | PXD017353 | Pride
Project description:The phytopathogen Xylella fastidiosa produces two classes of pili, long type IV pili and short type I pili, which are involved in motility and adhesion. In this work, we have investigated the role of Ï54 factor and its involvement in the regulation of fimbrial biogenesis in X. fastidiosa. An rpoN null mutant was constructed from citrus strain J1a12, and analyses of global gene expression profile by microarrays comparing the wild type and rpoN mutant strains showed that few genes exhibited differential expression. At least one gene, pilA1 (XF2542), which encodes the structural pilin protein of type IV fimbriae, showed decreased expression in the rpoN mutant whereas an operon encoding proteins of type I fimbriae were twofold more expressed in the mutant. Quantitative real time RT-PCR (qRT-PCR) analysis confirmed that pilA1 transcript was significantly reduced in the rpoN mutant. The transcriptional start site of pilA1 was determined by primer extension, and a canonical Ï54-dependent promoter was found upstream of the start site. Genome sequence analysis of X. fastidiosa revealed five paralogues of pilA, but microarray and qRT-PCR data demonstrated that only the pilA1 transcript was significantly affected in the rpoN mutant. The rpoN mutant made more biofilm than the wild type strain and presented a cell-cell aggregative phenotype. These results indicate that Ï54 regulates biofilm formation, probably via differential regulation of genes involved in type IV and type I fimbrial biogenesis. Direct comparison between wild type strain J1a12 and mutant strain rpoN-.
2010-06-25 | E-GEOD-8097 | biostudies-arrayexpress
Project description:Type IV Pili (T4P) are dynamic surface appendages that mediate adherence, motility, and DNA uptake in Kingella kingae, an important pediatric pathogen that causes osteoarticular infections, bacteremia, and endocarditis. While the major pilin subunit in K. kingae T4P is well characterized, the contribution of minor pilins to T4P structure and function remains unknown. Here, we used proteomics, molecular genetics, biochemical analyses, and structural modeling to identify and characterize all eight minor pilins in K. kingae. We identified a conserved operon of core minor pilin genes encoding FimT, PilV, PilW, PilX, and PilE that promotes surface piliation, adherence to epithelial cells, twitching motility, and natural transformation. Deletion of the fimTpilVWXE locus phenocopied loss of the PilC1 and PilC2 adhesins, and AlphaFold modeling combined with bacterial two-hybrid analysis suggested that FimT, PilV, PilW, and PilX form a complex at the pilus tip. The PilA2, ComP, and KK03_01180 minor pilins were dispensable for adherence and motility but promoted natural transformation and formed protein-protein interactions with the major pilin, suggesting that these proteins are incorporated throughout the pilus shaft. These findings support a new model for the architecture of the K. kingae type IV pilus, with distinct minor pilins localizing to different sites on the pilus fiber and mediating specialized functions essential for virulence.
2025-10-06 | PXD068177 | Pride
Project description:Pseudomonas aeruginosa lasR QS network promotes phage infection by regulating the biosynthesis of LPS and type IV pili by regulating the biosynthesis of LPS and type IV pili
| PRJNA1034550 | ENA
Project description:Piloerection (goosebump) requires concerted actions of the hair follicle, the arrector pili muscle (APM), and the sympathetic nerve, providing a model to study interactions across epithelium, mesenchyme, and nerves. Here, we show that APMs and sympathetic nerves form a dual component niche to modulate hair follicle stem cell (HFSC) activity. Sympathetic nerves form synapse-like structures with HFSCs and regulate HFSCs through norepinephrine, whereas APMs maintain sympathetic innervation to HFSCs. Without norepinephrine signaling, HFSCs enter a deep quiescence state by down-regulating cell cycle machinery and mitochondria metabolism, while up-regulating quiescence regulators Lhx2, Foxp1, and Fgf18. During development, HFSC progeny secrets Sonic Hedgehog (SHH) to direct the formation of this APM-sympathetic nerve niche, which in turn controls hair follicle regeneration in adults. Our results reveal a reciprocal interdependence between a regenerative tissue and its niche at different stages, and illustrate that nerves can modulate stem cell quiescence through synapses and neurotransmitters.
2020-07-15 | GSE130240 | GEO
Project description:Sympathetic nerves and arrector pili muscles form a dual component niche to regulate hair follicle stem cells
| PRJNA534427 | ENA
Project description:Francisella tularensis is a highly pathogenic intracellular bacterium that causes the disease tularemia. While its ability to replicate within cells has been studied in much detail, the bacterium also encodes a less characterised type 4 pili (T4P) system. T4Ps are dynamic adhesive organelles identified as major virulence determinants in many human pathogens. In F. tularensis, the T4P is required for adherence to the host cell, as well as for protein secretion. Several components, including pilins, a pili peptidase, a secretin pore and two ATPases, are required to assemble a functional T4P, and these are encoded within distinct clusters on the Francisella chromosome. While some of these components have been functionally characterised, the role of PilO, if any, still is unknown. Here, we examined the role of PilO in the pathogenesis of F. novicida. Our results show that the PilO is essential for pilus assembly on the bacterial surface. In addition, PilO is important for adherence of F. novicida to human monocyte-derived macrophages, secretion of effector proteins and intracellular replication. Importantly, the pilO mutant is attenuated for virulence in BALB/c mice regardless of the route of infection. Following intratracheal and intradermal infection, the mutant caused no histopathology changes, and demonstrated impaired phagosomal escape and replication within lung liver as well as spleen. Thus, PilO is an essential virulence determinant of F. novicida.
| S-EPMC8789160 | biostudies-literature