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Porin-mediated passage of negamycin across the outer membrane of Escherichia coli

ABSTRACT: Porin-mediated passage of negamycin across the outer membrane of Escherichia coli

PROVIDER: PRJNA760441 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15712276.fastq.gz	Fastqsanger.gz
	SRR15712277.fastq.gz	Fastqsanger.gz
	SRR15712278.fastq.gz	Fastqsanger.gz
	SRR15712279.fastq.gz	Fastqsanger.gz
	SRR15712280.fastq.gz	Fastqsanger.gz

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Porin-mediated passage of negamycin across the outer membrane of Escherichia coli

Project description:The rise of antimicrobial resistant pathogens calls for new antibacterial treatments, but potent new compounds are scarce. Development of new antibiotics is difficult, especially against Gram-negative bacteria, as here uptake is strongly hindered by the additional outer membrane. Most antimicrobial agents against Gram-negatives use the porin mediated pathway to cross the outer membrane, which limits the choice of an antibiotic, as it has to fit by size, charge and hydrophilicity. In E. coli, the major porins OmpF and OmpC are associated with antibiotic translocation and therefore also with unspecific antibiotic cross-resistance. In this regard, alternative uptake routes are of interest. We were interested in the uptake opportunities of the small, natural product antibiotic negamycin and thereby found new uptake pathways across the outer membrane of E. coli. Besides OmpF and OmpC, we investigated the role of the minor porins OmpN and ChiP in negamycin translocation. We detected an effect of OmpN and ChiP on negamycin susceptibility and confirmed passage by electrophysiological assays. The structure of OmpN was resolved in order to analyze the negamycin translocation mechanism by computational simulations. As abundancy of these minor porins was low in E. coli, their transcript levels were analyzed by RNA-Seq. Increased transcripts levels of ompN and chiP were observed upon negamycin treatment, hinting at a role in antibiotic uptake. These new, additional uptake pathways across the outer membrane of E. coli highlight the antibiotic potential of negamycin, especially as resistance development is low due to availability of multiple uptake routes at both the outer and inner membranes

2023-10-01 | GSE183363 | GEO

Fosfomycin uptake in Escherichia coli is mediated by the outer membrane porins OmpF, OmpC and LamB

Project description:The antibiotic fosfomycin is widely recognized for treatment of lower urinary tract infections caused by Escherichia coli and lately gained importance as a therapeutic option to combat multidrug resistant bacteria. Still, resistance to fosfomycin frequently develops through mutations reducing its uptake. Whereas the inner membrane transport of fosfomycin has been extensively studied in E. coli, its outer membrane (OM) transport remains insufficiently understood. While evaluating minimal inhibitory concentrations in OM porin-deficient mutants, we observed that the E. coli ΔompCΔompF strain is five times more resistant to fosfomycin than the wild type and the respective single mutants. Continuous monitoring of cell lysis of porin-deficient strains in response to fosfomycin additionally indicated the relevance of LamB. Furthermore, the physiological relevance of OmpF, OmpC and LamB for fosfomycin uptake was confirmed by electrophysiological and transcriptional analysis. This study expands the knowledge of how fosfomycin crosses the OM of E. coli.

2024-01-24 | GSE236554 | GEO

Fosfomycin uptake in Escherichia coli is mediated by the outer membrane porins OmpF, OmpC and LamB

Project description:Fosfomycin uptake in Escherichia coli is mediated by the outer membrane porins OmpF, OmpC and LamB

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An outer membrane porin-lipoprotein complex modulates elongasome movement to establish cell curvature in Rhodospirillum rubrum

Project description:Curved cell shapes are widespread among bacteria and important for cellular motility, virulence and fit-ness. However, the underlying morphogenetic mechanisms are still incompletely understood. Here, we identify an outer-membrane protein complex that promotes cell curvature in the pho¬tosynthetic species Rhodo¬spirillum rubrum. We show that the R. rubrum porins Por39 and Por41 form helical ribbon-like struc-tures at the outer curve of the cell that recruit the peptido¬glycan-binding lipo¬pro¬tein PapS, with PapS in-activation, porin de¬localization or disruption of the porin-PapS interface resulting in cell straight¬ening. We further demonstrate that porin-PapS assemblies act as molecular cages that entrap the cell elon¬gation ma-chine¬ry, thus biasing cell growth towards the outer curve. These findings reveal a mechanistically dis¬tinct mor¬pho¬genetic module medi¬ating bacterial cell shape. Moreover, they uncover an unprecedented role of outer-mem¬brane pro¬tein pat¬terning in the spatial control of intracellular processes, adding an important facet to the reper¬toire of regu¬la¬tory mechanisms in bac¬terial cell biology.

2024-07-17 | PXD049473 | Pride

Acetylome reveals the lysine acetylation modifications on outer membrane protein Aha1 in Aeromonas hydrophila regulate the porin permeability to multidrug antibiotics

Project description:Acetylome reveals the lysine acetylation modifications on outer membrane protein Aha1 in Aeromonas hydrophila regulate the porin permeability to multidrug antibiotics

2022-04-28 | PXD028447 |

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Project description:Endospore formation in Firmicutes is a complex morphological process triggered by environmental stress. At the end of this process, a mature spore containing the condensed genome is released through lysis of the mother cell. The mature spore is encased by several protective layers, including an inner and an outer spore membrane (IsM and OsM, respectively), both derived from the inner membrane (IM) of the mother cell. While this process is well understood in monoderm bacteria like Bacillus subtilis, less is known about diderm spore-formers such as Acetonema longum, which retain and remodel their OsM into a true outer membrane (OM) during germination. Our results show that outer membrane proteins (OMPs), including the essential β-barrel Assembly Machinery (BAM) component BamA, are present in vegetative and germinating cells but absent from mature spores. These observations highlight an unprecedented mechanism of inner to outer membrane remodelling in the absence of BamA. Expression profiles of cells at different growth stages and phylogenomic analyses identified two novel proteins, co-expressed and in an operon with BamA, that were highly conserved among diderm Firmicutes: a β-barrel OMP containing three polypeptide transport-associated (POTRA) domains (SonA) and a putative OM lipoprotein (SonB). In vitro experiments further demonstrated that both BamA and SonA can self-insert into liposomes under physiological conditions. Together, we propose a model in which BamA and its functional partners, SonA and SonB, drive membrane remodelling during germination. The process is initiated by self-insertion of BamA, which then assists the folding and insertion of other OMPs, including LptD, progressively shifting the protein and lipid composition of the OsM to produce a true OM. Collectively, our findings provide new insights into the functional role of BamA in membrane remodelling during OM biogenesis.

2025-09-06 | GSE306945 | GEO

Molecular interplay between peptidoglycan integrity and outer membrane asymmetry in maintaining cell envelope homeostasis

Project description:Loss of LdtJ in Acinetobacter baumannii disrupts cell morphology, downregulates peptidoglycan precursor genes (e.g., dadA, alr), and activates the stringent response, including elevated ppGpp levels and dksA upregulation. These defects are fully suppressed in a ∆ldtJ ∆mla double mutant, implicating the outer membrane lipid transport Mla pathway in compensatory regulation. RNA sequencing revealed that transcriptional changes in the ∆ldtJ mutant are reversed in the double mutant, highlighting a functional interplay between peptidoglycan remodeling and outer membrane lipid asymmetry.

2025-09-11 | GSE304602 | GEO

Exposure of bronchial airway epithelial cells to elexacaftor/tezacaftor/ivacaftor, Pseudomonas aeruginosa strain PA14 and outer membrane vesicles

Project description:Elexacaftor/tezacaftor/ivacaftor (ETI, Trikafta) is highly effective treatment for many cystic fibrosis patients, at least partly because it increases CFTR mediated Cl- and HCO3- secretion by airway epithelial cells leading to improved lung function and less frequent exacerbations and hospitalizations. However, little is known about how ETI affects airway epithelial cells in ways not related to CFTR mediated Cl- and HCO3- secretion, for example how ETI affects the expression of genes other than CFTR or how ETI might affect airway cells’ response to infection. It is established that CF airway cells bearing the delta F 508 mutation the CFTR gene respond characteristically differently from wild type CFTR cells, and we hypothesized that, as a highly effective CFTR modulator, ETI might make airway cells from CF donors respond to pathogen stimulation (Pseudomonas aeruginosa PA14 or outer membrane vesicles isolated from these bacteria) in more the same way that cells from wild type, healthy control cells do. We tested this hypothesis by measuring gene expression responses in polarized primary CF airway cells exposed to ETI alone or ETI in the presence of a pathogen challenge (PA14 or outer membrane vesicles). Responses of CFTR wild type primary CF airway cells to PA14 or outer membrane vesicles was also measured for comparison

2024-06-25 | GSE268718 | GEO

mRNA transcript distribution bias between Borrelia burgdorferi bacteria and their outer membrane vesicles

Project description:We performed comparative transcriptomic analysis of the outer membrane vesicles (OMVs) released from B. burgdorferi. We identified a total of ~1200 unique transcripts with at least one mapped read from the bacterial cell and its OMVs.

2018-06-21 | GSE114368 | GEO

Influence of quorum sensing on Klebsiella pneumoniae outer membrane vesicles

Project description:Influence of quorum sensing on Klebsiella pneumoniae outer membrane vesicles

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