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Wamp, S.

Publications and source records attributed to Wamp, S..

9 recordsLinked to original sources

On the role of cell chaining in the attenuation of a Listeria monocytogenes divIVA mutant

Listeria monocytogenes is a facultative intracellular human pathogen capable of invading non-phagocytic host cells, replicating within their cytosol, and spreading directly from cell to cell. These processes are mediated by specialized virulence factors but also depend on the DivIVA protein. DivIVA aids in the secretion of peptidoglycan-degrading autolysins in a process that requires the accessory secretion ATPase SecA2, thereby promoting daughter cell separation following cytokinesis. Consequently, a {Delta}divIVA mutant forms elongated chains of unseparated daughter cells, which may explain its attenuated virulence. To further explore the role of cell chaining for attenuation, we here investigated how different morphological aberrations affect the virulence of L. monocytogenes. To this end, we generated coccoid mreB and filamentous ezrA mutants, and compared them to the {Delta}divIVA mutant in different in vitro infection assays. Coccoid or filamentous morphologies did not impair host cell invasion or intracellular replication, unlike cell chaining of the {Delta}divIVA mutant. Introduction of a hyperactive allele of the PrfA virulence regulator, resulting in constitutive overexpression of virulence genes, was sufficient to restore the invasion defect of the {Delta}divIVA mutant, despite its pronounced cell chaining phenotype, but did not recover intracellular replication. We isolated suppressors of the {Delta}divIVA mutant carrying mutations in secA2, which likely enhance the SecA2 ATPase activity. In these suppressors, autolysin secretion, daughter cell separation, and invasion were fully restored, and intracellular replication was partially recovered. Thus, maintaining normal rod-shaped morphology plays a minor role in L. monocytogenes pathogenesis. Instead, virulence attenuation in the {Delta}divIVA mutant is better explained by distortions in PrfA- and SecA2-dependent processes. Author SummaryListeria monocytogenes infects humans by entering host cells, replicating intracellularly, and spreading from infected cells to neighboring cells. The bacterium is rod-shaped and normally occurs as single or double cells that can efficiently complete all stages of infection. However, a class of virulence-attenuated L. monocytogenes mutants forms long cell chains, suggesting a link between cell morphology and virulence. One such mutant lacks the cell division protein DivIVA and is severely impaired in infection, as it neither invades host cells, replicates in the cytoplasm nor spreads from cell to cell. To determine whether virulence attenuation is caused by cell chaining itself or by additional functional defects, we compared the virulence of the divIVA mutant with that of mutants exhibiting other morphological abnormalities. In addition, we isolated suppressor mutations that restore normal cell separation in the divIVA mutant and examined their effects on virulence. Our results show that cell morphology per se does not generally determine listerial virulence. Instead, they indicate that specific virulence-related functions are impaired in chain-forming L. monocytogenes mutants. These findings advance our understanding of the virulence defects associated with cell chaining and provide a basis for identifying their real underlying molecular causes.

microbiology↗

Three pathways feed the folate-dependent one carbon pool for growth and virulence of Listeria monocytogenes

The bacterium Listeria monocytogenes can grow in the cytoplasm of infected human cells, but there it relies on specific biosynthetic pathways for intracellular nutrient supply. We previously found that the glycine cleavage system (GCS) is needed for intracellular growth. The GCS decarboxylates glycine for generation of 1C-tetrahydrofolates (1C-THF), folate-dependent one carbon donors needed for biosynthesis of other metabolites. We continued our studies on the GCS and show that a L. monocytogenes {Delta}gcvPAB mutant, lacking the GCS glycine dehydrogenase, is attenuated without resembling the phenotype of classical virulence factor mutants. The {Delta}gcvPAB mutant also grew poorly in synthetic medium, explained by the presence of glycine that was toxic for this strain. Selection of glycine resistant suppressors yielded a survivor, in which the N- and C-terminal parts of the formate-tetrahydrofolate ligase (fhs) gene, which is naturally separated into two parts by a premature stop codon in the L. monocytogenes reference strain EGD-e, were reassembled into a full-length open reading frame. Like the GCS, Fhs also feeds the 1C-THF pool and its restoration cured the virulence defects of the {Delta}gcvPAB mutant. Another suppressor had a mutated glyA gene, encoding serine hydroxymethyltransferase, and combinatorial deletions of gcvPAB and glyA in fhs- and fhs+ backgrounds demonstrated a role of GlyA in 1C-THF metabolism. Our results show that three pathways feed the 1C-THF pool to support growth and virulence of L. monocytogenes and represent the first example of the spontaneous reactivation of a L. monocytogenes gene that is inactivated by a premature stop codon.

microbiology↗

A pbpB1 mutation causing β-lactam resistance in clinical Listeria monocytogenes isolates

ObjectivesListeriosis is a severe foodborne infection and associated with high mortality. Treatment is based on ampicillin, amoxicillin or penicillin, often combined with gentamicin, but meropenem is also used occasionally. {beta}-lactam resistant Listeria monocytogenes isolates are infrequently described but the mechanism of resistance is not known. MethodsA clinical L. monocytogenes isolate with suspected {beta}-lactam resistance was collected from a German listeriosis patient. Resistance profiling, whole genome sequencing, comparative genomics and genetic experiments were used to identify the causative DNA polymorphism. Spontaneous ampicillin resistant suppressors of L. monocytogenes reference strain EGD-e were selected and their genomes sequenced. ResultsA W428R substitution near the active site of penicillin binding protein B1 (PBP B1) was identified as the cause of ampicillin, amoxicillin and meropenem resistance. Further clinical L. monocytogenes isolates with similar resistance profiles were found by searching the genome database of the German consultant laboratory for Listeria for pbpB1 W428R-positive isolates. Furthermore, the same mutation was selected for in strain EGD-e during cultivation in the presence of ampicillin. ConclusionsL. monocytogenes can develop {beta}-lactam resistance by a specific substitution in PBP B1, likely selected for during {beta}-lactam treatment. Antibiotic susceptibility testing should be considered an important part of adequate listeriosis therapy.

microbiology↗

Cytosolic factors controlling PASTA kinase-dependent ReoM phosphorylation

Bacteria adapt the biosynthesis of their envelopes to specific growth conditions and prevailing stress factors. Peptidoglycan (PG) is the major component of the cell wall in Gram-positive bacteria, where PASTA kinases play a central role in PG biosynthesis regulation. Despite their importance for growth, cell division and antibiotic resistance, the mechanisms of PASTA kinase activation are not fully understood. ReoM, a recently discovered cytosolic phosphoprotein, is one of the main substrates of the PASTA kinase PrkA in the Gram-positive human pathogen Listeria monocytogenes. Depending on its phosphorylation, ReoM controls proteolytic stability of MurA, the first enzyme in the PG biosynthesis pathway. The late cell division protein GpsB has been implicated in PASTA kinase signalling. Consistently, we show that L. monocytogenes prkA and gpsB mutants phenocopied each other. Analysis of in vivo ReoM phosphorylation confirmed GpsB as an activator of PrkA leading to the description of structural features in GpsB that are important for kinase activation. We further show that ReoM phosphorylation is growth-phase dependent and that this kinetic is reliant on the protein phosphatase PrpC. ReoM phosphorylation was inhibited in mutants with defects in MurA degradation, leading to the discovery that artificial MurA overexpression prevented ReoM phosphorylation. Overexpressed MurA must adopt its substrate-bound closed conformation and interact with ReoM to exert this effect, but the extracellular PASTA domains of PrkA or MurJ flippases where not required. Our results indicate that intracellular signals control ReoM phosphorylation and extend current models describing the mechanisms of PASTA kinase activation.

microbiology↗

High density genomic surveillance and risk profiling of clinical Listeria monocytogenes subtypes in Germany, 2018-2021

AO_SCPLOWBSTRACTC_SCPLOWFoodborne infections represent a significant public health concern, particularly when outbreaks affect many individuals over prolonged time. Systematic collection of pathogen isolates from infected patients, whole genome sequencing and phylogenetic analyses allow recognition and termination of outbreaks after source identification and risk profiling of abundant lineages. We here present a multi-dimensional analysis of >1,800 genome sequences from clinical L. monocytogenes isolates collected in Germany between 2018-2021. These isolates covered 62% of all notified cases and belonged to 188 infection clusters. 42% of these clusters were active for >12 months, 60% generated cases cross-regionally, including 11 multinational clusters. 37% of the clusters were caused by sequence type (ST) ST6, ST8 and ST1 clones and for selected clusters, we provide further epidemiological and genetic information. Frequencies of materno-fetal and brain infections allowed risk profiling of the most abundant STs, differentiating ST1 as hyper- and ST8, ST14, ST29 as well as ST155 as hypovirulent from ST6 with average virulence potential. Hepatocyte infection experiments confirmed these virulence differences. Inactivating mutations were found in several virulence and house-keeping genes, particularly in hypovirulent STs. Our work supports prioritization of clusters for epidemiological investigations and reinforces the need to analyse the mechanisms underlying hyper- and hypovirulence.

microbiology↗

Structure-function relationships underpin disulfide loop cleavage-dependent activation of Legionella pneumophila lysophosholipase A PlaA

Legionella pneumophila, the causative agent of a life-threatening pneumonia, intracellularly replicates in a specialized compartment in lung macrophages, the Legionella-containing vacuole (LCV). Secreted proteins of the pathogen govern important steps in the intracellular life cycle including bacterial egress. Among these is the type II secreted PlaA which, together with PlaC and PlaD, belongs to the GDSL phospholipase family found in L. pneumophila. PlaA shows lysophospholipase A (LPLA) activity which increases after secretion and subsequent processing by the zinc metalloproteinase ProA at residue E266/L267 located within a disulfide loop. Activity of PlaA contributes to the destabilization of the LCV in the absence of the type IVB-secreted effector SdhA. We here present the 3D structure of PlaA which shows a typical /{beta} hydrolase fold and reveals that the uncleaved disulfide loop forms a lid structure covering the catalytic triad S30/D278/H282. This leads to reduction of both substrate access and membrane interaction before activation; however, the catalytic and membrane interaction site gets more accessible when the disulfide loop is processed. After structural modelling, a similar activation process is suggested for the GDSL hydrolase PlaC, but not for PlaD. Furthermore, the size of the PlaA substrate binding site indicated preference towards phospholipids comprising ~16 carbon fatty acid residues which was verified by lipid hydrolysis, suggesting a molecular ruler mechanism. Indeed, mutational analysis changed the substrate profile with respect to fatty acid chain length. In conclusion, our analysis revealed the structural basis for the regulated activation and substrate preference of PlaA.

biochemistry↗

MurA escape mutations uncouple peptidoglycan biosynthesis from PrkA signaling

Gram-positive bacteria are protected by a thick mesh of peptidoglycan (PG) completely engulfing their cells. This PG network is the main component of the bacterial cell wall, it provides rigidity and acts as foundation for the attachment of other surface molecules. Biosynthesis of PG consumes a high amount of cellular resources and therefore requires careful adjustments to environmental conditions. An important switch in the control of PG biosynthesis of Listeria monocytogenes, a Gram-positive pathogen with a high infection fatality rate, is the serine/threonine protein kinase PrkA. A key substrate of this kinase is the small cytosolic protein ReoM. We have shown previously that ReoM phosphorylation regulates PG formation through control of MurA stability. MurA catalyzes the first step in PG biosynthesis and the current model suggests that phosphorylated ReoM prevents MurA degradation by the ClpCP protease. In contrast, conditions leading to ReoM dephosphorylation stimulate MurA degradation. How ReoM controls degradation of MurA and potential other substrates is not understood. Also, the individual contribution of the [~]20 other known PrkA targets to PG biosynthesis regulation is unknown. We here present murA mutants which escape proteolytic degradation. The release of MurA from ClpCP-dependent proteolysis was able to constitutively activate PG biosynthesis and further enhances the intrinsic cephalosporin resistance of L. monocytogenes. This activation required the RodA3/PBP B3 transglycosylase/transpeptidase pair as additional effectors of the PrkA signaling route. One murA escape mutation not only fully rescued an otherwise non-viable prkA mutant during growth in batch culture and inside macrophages but also overcompensated cephalosporin hypersensitivity. Our data collectively indicate that the main purpose of PrkA-mediated signaling in L. monocytogenes is control of MurA stability during extra- and intracellular growth. These findings have important implications for the understanding of PG biosynthesis regulation and {beta}-lactam resistance of L. monocytogenes and related Gram-positive bacteria. Author SummaryPeptidoglycan (PG) is the main component of the bacterial cell wall and many of the PG synthesizing enzymes are antibiotic targets. We previously have discovered a new signaling route controlling PG production in the human pathogen Listeria monocytogenes. This route also determines the intrinsic resistance of L. monocytogenes against cephalosporins, a group of {beta}-lactam antibiotics. Signaling involves PrkA, a membrane-embedded protein kinase, that is activated during cell wall stress to phosphorylate its target ReoM. Depending on its phosphorylation, ReoM activates or inactivates PG production by controlling the proteolytic stability of MurA, which catalyzes the first step in PG biosynthesis. MurA degradation depends on the ClpCP protease and we here have isolated murA mutations that escape this degradation. Using these mutants, we could show that regulation of PG biosynthesis through control of MurA stability is the primary purpose of PrkA-mediated signaling in L. monocytogenes. Further experiments identified the transglycosylase RodA and the transpeptidase PBP B3 as additional effectors of PrkA signaling. Our results suggest that both proteins act together to translate the signals received by PrkA into intensification of PG biosynthesis. These findings shed new light on the regulation of PG biosynthesis in Gram-positive bacteria with intrinsic {beta}-lactam resistance.

microbiology↗

Population structure-guided profiling of antibiotic resistance patterns in clinical Listeria monocytogenes isolates from Germany identifies pbpB3 alleles associated with low levels of cephalosporin resistance

AO_SCPLOWBSTRACTC_SCPLOWCase numbers of listeriosis have been increasing in Germany and the European Union during the last decade. In addition reports on the occurrence of antibiotic resistance in Listeria monocytogenes in clinical and environmental isolates are accumulating. The susceptibility towards 14 antibiotics was tested in a selection of clinical L. monocytogenes isolates to get a more precise picture of the development and manifestation of antibiotic resistance in the L. monocytogenes population. Based on the population structure determined by core genome multi locus sequence typing (cgMLST) 544 out of 1,220 sequenced strains collected in Germany between 2009 and 2019 were selected to cover the phylogenetic diversity observed in the clinical L. monocytogenes population. All isolates tested were susceptible towards ampicillin, penicillin and co-trimoxazole - the most relevant antibiotics in the treatment of listeriosis. Resistance to daptomycin and ciprofloxacin was observed in 493 (91%) and in 71 (13%) of 544 isolates, respectively. While all tested strains showed resistance towards ceftriaxone, the minimal inhibitory concentrations (MIC) observed varied widely between 4 mg/L up to >128 mg/L. An allelic variation of the penicillin binding protein gene pbpB3 could be identified as the cause of this difference in ceftriaxone resistance levels. This study is the first population structure-guided analysis of antimicrobial resistance in recent clinical isolates and confirms the importance of penicillin binding protein B3 (PBP B3) for the high level of intrinsic cephalosporin resistance of L. monocytogenes on a population-wide scale.

microbiology↗

Bacterial cell wall integrity surveillance is connected to peptidoglycan biosynthesis by the essential phosphorylation of ReoM

Peptidoglycan (PG) is the main component of bacterial cell walls and the target for many antibiotics. PG biosynthesis is tightly coordinated with cell wall growth and turnover, and many of these control activities depend upon PASTA-domain containing eukaryotic-like serine/threonine protein kinases (PASTA-eSTK) that sense PG fragments. However, only a few PG biosynthetic enzymes are direct kinase substrates. Here, we identify the conserved ReoM protein as a novel PASTA-eSTK substrate in the Gram-positive pathogen Listeria monocytogenes. Our data show that the phosphorylation of ReoM is essential as it controls ClpCP-dependent proteolytic degradation of the essential enzyme MurA, which catalyses the first committed step in PG biosynthesis. We also identify ReoY as a second novel factor required for degradation of ClpCP substrates. Collectively, our data imply that the first committed step of PG biosynthesis is activated through control of ClpCP protease activity in response to signals of PG homeostasis imbalance.

microbiology↗