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Aduse-Opoku, J.

Publications and source records attributed to Aduse-Opoku, J..

3 recordsLinked to original sources

The Porphyromonas gingivalis lipid A 1-phosphatase LpxE has unique features and requires a functional type IX secretion system for its activity

Porphyromonas gingivalis is a Gram-negative bacterium that plays a central role in the development of periodontal disease. It uses a type IX secretion system (T9SS) to export a range of virulence factors to the bacterial surface where they are attached to A-LPS, one of the two forms of lipopolysaccharide (LPS) produced in P. gingivalis, and then packaged into outer membrane vesicles (OMVs). We previously showed that 1-P dephosphorylation of the lipid A component of LPS is regulated by the T9SS outer membrane protein (OMP) PorV, and this is linked to membrane destabilisation and OMV blebbing/formation. In this study we aimed to extend this and investigate the role of other T9SS OMPs in OMV biogenesis. We examined gingipain activity, gingipain secretion, A-LPS production, OMV morphology, and lipid A structure in P. gingivalis W50 and T9SS OMP mutant strains, and our results support an essential role for these proteins in type IX secretion. In addition, we produced a lipid A 1-phosphatase ({Delta}lpxE) mutant and show that all T9SS OMPs are required for LpxE activity and correct vesicle formation. LpxE has a unique C-terminal extension, and we propose that a cargo protein exported by the T9SS can directly/indirectly interact with this and regulate LpxE activity. This study provides insight into a new mechanism that links type IX cargo sorting with OMV blebbing, which may also be present in other Bacteroidota that colonise the gut and oral cavity.

microbiology↗

Hemin availability induces coordinated DNA methylation and gene expression changes in Porphyromonas gingivalis

Periodontal disease is a common chronic inflammatory disease. Porphyromonas gingivalis is an important bacterium in the development of the disease and expresses a variety of virulence determinants. Hemin (iron [III] protopotphyrin IX), an essential nutrient of this organism, whose concentration increases with increasing inflammation, is a global regulator of virulence in P. gingivalis: high hemin levels increase expression of several virulence determinants. However, the mechanism through which hemin influences bacterial gene expression is poorly understood. Bacterial DNA methylation has the potential to fulfil this mechanistic role. Here, we characterised the methylome of P. gingivalis, and compared its variation to transcriptomic changes in response to changes in hemin concentration. Gene expression and DNA methylation profiling of P. gingivalis W50 was performed, following continuous culture in chemostats with excess or limited hemin, using Illumina RNA-Seq and Nanopore DNA sequencing. DNA methylation quantification was carried out for Dam/Dcm motifs and all-context N6-methyladenine (6mA) and 5-methylcytosine (5mC) base pair modifications. Differential expression and methylation in response to excess hemin availability are presented after multiple testing correction (FDR 5%). In excess hemin there were 161 over- and 268 under-expressed genes compared to limited hemin. Genes under-expressed in excess hemin were involved in iron recruitment (the hemophore HmuY) and transport (TonB-dependent receptors), and those over-expressed were involved in iron-sulphur cluster binding. Hemin-dependent differentially methylation was observed for the Dam GATC motif and all-context 6mA and 5mC, with 36, 49 and 47 signals, respectively. Coordinated genome-wide differential expression and methylation effects were observed in 6 genes encoding a Ppx/GppA family phosphatase, a lactate utilization protein, a 4-alpha-glucanotransferase, two ABC transporter proteins, and a hypothetical protein HMPREF1322_RS00730. The findings indicate that altered genome methylation occurs in response to the availability of hemin and give insights into the molecular mechanisms of regulation of virulence in this bacterium. Author SummaryDNA methylation has important roles in bacteria, including in the regulation of transcription. Porphyromonas gingivalis, an oral pathogen in periodontitis, exhibits well-established gene expression changes in response to hemin availability. However, the gene regulatory processes underlying these effects remain unknown. To this end, we profiled the novel P. gingivalis epigenome, and assessed epigenetic and transcriptome variation under limited and excess hemin conditions. As expected, multiple gene expression changes were detected in response to limited and excess hemin conditions that reflect conditions associated with health and disease, respectively. Notably, we also detected differential DNA methylation signatures for the Dam GATC motif and both all-context N6-methyladenine (6mA) and 5-methylcytosine (5mC) in response to hemin availability. Joint analyses identified a subset of coordinated changes in gene expression, 6mA, and 5mC methylation that target genes involved in lactate utilization and ABC transporters. The results identify novel regulatory processes underlying the mechanism of hemin regulated gene expression in P. gingivalis, with phenotypic impacts on its virulence in periodontal disease.

genomics↗

The essential Porphyromonas gingivalis type IX secretion system component PorZ delivers anionic-lipopolysaccharide to the PorU sortase for transpeptidase processing of cargos

Cargo proteins of the type IX secretion system (T9SS) in human pathogens from phylum Bacteroidetes invariably possess a conserved C-terminal domain (CTD) that functions as a signal for outer membrane (OM) translocation. In Porphyromonas gingivalis, the CTD of selected cargos is cleaved off after translocation, and anionic lipopolysaccharide (A-LPS) is attached. This transpeptidase reaction anchors secreted proteins to the OM. PorZ, a cell surface-associated protein, is an essential component of the T9SS whose function was previously unknown. We recently solved the crystal structure of PorZ, and found that it consists of two {beta}-propeller moieties followed by a CTD. In this study, we performed structure-based modelling suggesting that PorZ is a carbohydrate-binding protein. We found that recombinant PorZ specifically binds A-LPS. Binding was blocked by monoclonal antibodies that specifically react with a phosphorylated branched mannan in the anionic polysaccharide (A-PS) component of the A-LPS, but not with the core oligosaccharide or the lipid A endotoxin. Examination of A-LPS derived from a cohort of mutants producing various truncations of A-PS confirmed that the phosphorylated branched mannan is indeed the PorZ ligand. Moreover, purified recombinant PorZ interacted with the PorU sortase in an A-LPS-dependent manner. This interaction on the cell surface is crucial for the function of the attachment complex composed of PorU, PorZ, and the integral OM {beta}-barrel proteins PorV and PorQ, which is involved in post-translational modification and retention of T9SS cargos on the bacterial surface. Author summaryBacteria have evolved multiple systems to transport effector proteins to their surface or into the surrounding milieu. These proteins have a wide range of functions, including attachment, motility, nutrient acquisition, and toxicity in the host. Porphyromonas gingivalis, the human pathogen responsible for severe gum diseases (periodontitis), uses a recently characterized type IX secretion system (T9SS) to translocate and anchor secreted virulence effectors to the cell surface. Anchorage is facilitated by sortase, an enzyme that covalently attaches T9SS cargo proteins to a unique anionic lipopolysaccharide (A-LPS) moiety of P. gingivalis. Here, we show that the T9SS component PorZ interacts with sortase and specifically binds A-LPS. Binding is mediated by a phosphorylated branched mannan repeat in A-LPS polysaccharide. A-LPS- bound PorZ interacts with sortase with significantly greater affinity, facilitating modification of cargo proteins by the cell-surface attachment complex of the T9SS.

microbiology↗