Unconventional membrane lipid biosynthesis in <scp><i>X</i></scp><i>anthomonas campestris</i>

Aktas, Meriyem; Narberhaus, Franz

doi:10.1111/1462-2920.12956

Cited by 13 publications

(11 citation statements)

References 86 publications

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“…Those results suggested that fengycin and DPPC interact in the membrane. In agreement with the above mentioned, membranes of both Xav and PA01 strains used in this study contain PC, a phospholipid relatively unusual in bacteria (Geiger et al, 2003;Aktas and Narberhaus, 2015). Based on those studies and depending on the fengycin concentration, two mechanisms of action were proposed: under low fengycin concentrations, fengycin aggregates causing the formation of pores and the subsequent changes in membrane permeability, whereas, at high concentration, fengycin solubilize the membrane similarly as a detergent (Deleu et al, 2005(Deleu et al, , 2008.…”

Section: Discussionsupporting

confidence: 81%

Fengycins From Bacillus amyloliquefaciens MEP218 Exhibit Antibacterial Activity by Producing Alterations on the Cell Surface of the Pathogens Xanthomonas axonopodis pv. vesicatoria and Pseudomonas aeruginosa PA01

Medeot

Fernandez²,

Morales³

et al. 2020

Front. Microbiol.

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Section: Discussionsupporting

confidence: 81%

Fengycins From Bacillus amyloliquefaciens MEP218 Exhibit Antibacterial Activity by Producing Alterations on the Cell Surface of the Pathogens Xanthomonas axonopodis pv. vesicatoria and Pseudomonas aeruginosa PA01

Medeot

Fernandez²,

Morales³

et al. 2020

Front. Microbiol.

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“…Ultracentrifugation resulted in vesicle‐bound proteins floating in the upper fraction of the gradient, whereas unbound proteins remained in the lower fraction. First, we used liposomes similar to the standard lipid composition of Xanthomonas membranes, which mainly consist of ~50% phosphatidylethanolamine (PE), ~33% CL, ~13% phosphatidylglycerol (PG) and ~6% phosphatidylcholine (PC) (Aktas and Narberhaus, ). As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…This might be supported by the interaction with negatively charged membrane surfaces, which can also promote partial protein unfolding (Musatov and Sedlák, 2017). Xanthomonas membranes are rich in CL (Aktas and Narberhaus, 2015), a dimeric phospholipid potentially carrying two negative charges. Notably, CL binding of proteins is often attributed to regions rich in basic amino acids [Arg, histidine (His) and lysine (Lys)], which form a phosphate-binding patch (Musatov and Sedlák, 2017;Planas-Iglesias et al, 2015).…”

Section: Xopb Associates With the Bacterial Membranementioning

confidence: 99%

A conserved motif promotes HpaB‐regulated export of type III effectors from Xanthomonas

Prochaska

Thieme

Daum

et al. 2018

Molecular Plant Pathology

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The type III secretion (T3S) system, an essential pathogenicity factor in most Gram-negative plant-pathogenic bacteria, injects bacterial effector proteins directly into the plant cell cytosol. Here, the type III effectors (T3Es) manipulate host cell processes to suppress defence and establish appropriate conditions for bacterial multiplication in the intercellular spaces of the plant tissue. T3E export depends on a secretion signal which is also present in 'non-effectors'. The latter are secreted extracellular components of the T3S apparatus, but are not translocated into the plant cell. How the T3S system discriminates between T3Es and non-effectors is still enigmatic. Previously, we have identified a putative translocation motif (TrM) in several T3Es from Xanthomonas campestris pv. vesicatoria (Xcv). Here, we analysed the TrM of the Xcv effector XopB in detail. Mutation studies showed that the proline/arginine-rich motif is required for efficient type III-dependent secretion and translocation of XopB and determines the dependence of XopB transport on the general T3S chaperone HpaB. Similar results were obtained for other effectors from Xcv. As the arginine residues of the TrM mediate specific binding of XopB to cardiolipin, one of the major lipid components in Xanthomonas membranes, we assume that the association of T3Es to the bacterial membrane prior to secretion supports type III-dependent export.

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“…In the course of our studies on the heterogeneous and dynamically remodelled membrane lipid repertoire of plant pathogenic bacteria (Aktas et al ., 2014; Aktas and Narberhaus, 2015), we examined the lipid profile of A. tumefaciens in the presence of various exogenous L‐PLs. We observed the L‐PG‐dependent production of considerable amounts of two isomeric forms of the lipid bis(monoacylglycero)phosphate (BMP), which has been rarely described in bacteria.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of the unusual lipid bis(monoacylglycero)phosphate in environmental bacteria

Czolkoss

Borgert

Poppenga

et al. 2021

Environmental Microbiology

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Summary The bacterial membrane is constantly remodelled in response to environmental conditions and the external supply of precursor molecules. Some bacteria are able to acquire exogenous lyso‐phospholipids and convert them to the corresponding phospholipids. Here, we report that some soil‐dwelling bacteria have alternative options to metabolize lyso‐phosphatidylglycerol (L‐PG). We find that the plant‐pathogen Agrobacterium tumefaciens takes up this mono‐acylated phospholipid and converts it to two distinct isoforms of the non‐canonical lipid bis(monoacylglycero)phosphate (BMP). Chromatographic separation and quadrupole‐time‐of‐flight MS/MS analysis revealed the presence of two possible BMP stereo configurations acylated at either of the free hydroxyl groups of the glycerol head group. BMP accumulated in the inner membrane and did not visibly alter cell morphology and growth behaviour. The plant‐associated bacterium Sinorhizobium meliloti was also able to convert externally provided L‐PG to BMP. Other bacteria like Pseudomonas fluorescens and Escherichia coli metabolized L‐PG after cell disruption, suggesting that BMP production in the natural habitat relies both on dedicated uptake systems and on head‐group acylation enzymes. Overall, our study adds two previously overlooked phospholipids to the repertoire of bacterial membrane lipids and provides evidence for the remarkable condition‐responsive adaptation of bacterial membranes.

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Unconventional membrane lipid biosynthesis in Xanthomonas campestris

Cited by 13 publications

References 86 publications

Fengycins From Bacillus amyloliquefaciens MEP218 Exhibit Antibacterial Activity by Producing Alterations on the Cell Surface of the Pathogens Xanthomonas axonopodis pv. vesicatoria and Pseudomonas aeruginosa PA01

Fengycins From Bacillus amyloliquefaciens MEP218 Exhibit Antibacterial Activity by Producing Alterations on the Cell Surface of the Pathogens Xanthomonas axonopodis pv. vesicatoria and Pseudomonas aeruginosa PA01

A conserved motif promotes HpaB‐regulated export of type III effectors from Xanthomonas

Synthesis of the unusual lipid bis(monoacylglycero)phosphate in environmental bacteria

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