Role of Phosphoglucomutase of
            <i>Stenotrophomonas</i>
            <i>maltophilia</i>
            in Lipopolysaccharide Biosynthesis, Virulence, and Antibiotic Resistance

McKay, Geoffrey A.; Woods, Donald E.; MacDonald, Kelly L.; Poole, Keith

doi:10.1128/iai.71.6.3068-3075.2003

Cited by 81 publications

(78 citation statements)

References 66 publications

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“…As a result, lack of PGM activity often results in an incomplete core and the inability to attach O antigen to the LPS core. In many cases this is believed to be the cause of serum sensitivity and antimicrobial peptide sensitivity of PGM-negative strains (15,39,48,66,69). LPS from the KIM5 ⌬pgm strain had no alterations in LPS chemistry compared to the parental strain ( Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Glucose-1-phosphate is a precursor of UDP-glucose and UDP-galactose (78), which are precursors of carbohydrate-containing anionic envelope polymers such as LPS, teichoic acid, lipoteichoic acid, cyclic ␤-1,2-glucans, and exopolysaccharides (5,45,66,78). Deletion of the gene encoding PGM activity modestly increases antimicrobial peptide susceptibility of Streptococcus iniae (9), Brucella abortus (66), Bordetella bronchiseptica (69), and Stenotrophomonas maltophilia (48). In some cases, mutants lacking PGM activity are also defective for intracellular survival (9, 66, 69), serum resistance (9,15,39,48), and in vivo colonization and/or virulence (3,9,39,48,66,69).…”

Section: Discussionmentioning

confidence: 99%

“…Deletion of the gene encoding PGM activity modestly increases antimicrobial peptide susceptibility of Streptococcus iniae (9), Brucella abortus (66), Bordetella bronchiseptica (69), and Stenotrophomonas maltophilia (48). In some cases, mutants lacking PGM activity are also defective for intracellular survival (9, 66, 69), serum resistance (9,15,39,48), and in vivo colonization and/or virulence (3,9,39,48,66,69). In the absence of PGM, UDP-glucose and UDP-galactose cannot be incorporated into LPS (78).…”

Section: Discussionmentioning

confidence: 99%

“…These nucleotide sugars can then be used to elaborate sugar modifications on cellular components such as lipopolysaccharide ([LPS] particularly the core region), teichoic acid, and secreted matrix components. Loss of PGM activity in several organisms has been reported to increase their sensitivity to antimicrobial peptides (9,48,66,69), and PGM-dependent modifications of bacterial surfaces have been shown to be critical for virulence in a number of pathogenic organisms (3, 9, 39, 48, 66, 69), usually due to alterations ment was repeated for five consecutive days, and the enriched mutant population was plated on HIA. A total of 100 single colonies from enrichment steps were tested for autoaggregation.…”

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confidence: 99%

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Phosphoglucomutase ofYersinia pestisIs Required for Autoaggregation and Polymyxin B Resistance

et al. 2010

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Yersinia pestis, the causative agent of plague, autoaggregates within a few minutes of cessation of shaking when grown at 28°C. To identify the autoaggregation factor of Y. pestis, we performed mariner-based transposon mutagenesis. Autoaggregation-defective mutants from three different pools were identified, each with a transposon insertion at a different position within the gene encoding phosphoglucomutase (pgmA; y1258). Targeted deletion of pgmA in Y. pestis KIM5 also resulted in loss of autoaggregation. Given the previously defined role for phosphoglucomutase in antimicrobial peptide resistance in other organisms, we tested the KIM5 ⌬pgmA mutant for antimicrobial peptide sensitivity. The ⌬pgmA mutant displayed >1,000-fold increased sensitivity to polymyxin B compared to the parental Y. pestis strain, KIM5. This sensitivity is not due to changes in lipopolysaccharide (LPS) since the LPSs from both Y. pestis KIM5 and the ⌬pgmA mutant are identical based on a comparison of their structures by mass spectrometry (MS), tandem MS, and nuclear magnetic resonance analyses. Furthermore, the ability of polymyxin B to neutralize LPS toxicity was identical for LPS purified from both KIM5 and the ⌬pgmA mutant. Our results indicate that increased polymyxin B sensitivity of the ⌬pgmA mutant is due to changes in surface structures other than LPS. Experiments with mice via the intravenous and intranasal routes did not demonstrate any virulence defect for the ⌬pgmA mutant, nor was flea colonization or blockage affected. Our findings suggest that the activity of PgmA results in modification and/or elaboration of a surface component of Y. pestis responsible for autoaggregation and polymyxin B resistance.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Phosphoglucomutase ofYersinia pestisIs Required for Autoaggregation and Polymyxin B Resistance

et al. 2010

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“…campestris and 72% identity with spgM (GenBank accession no. AY179964) in S. maltophilia K1014 (24).…”

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confidence: 99%

Differential Biofilm Formation and Motility Associated with Lipopolysaccharide/Exopolysaccharide-Coupled Biosynthetic Genes inStenotrophomonas maltophilia

2006

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Stenotrophomonas maltophilia WR-C is capable of forming biofilm on polystyrene and glass. The lipopolysaccharide/exopolysaccharide-coupled biosynthetic genes rmlA, rmlC, and xanB are necessary for biofilm formation and twitching motility. Mutants with mutations in rmlAC and xanB display contrasting biofilm phenotypes on polystyrene and glass and differ in swimming motility.Microorganisms can develop biofilms or clogging mats, causing the failure of septic tanks, systems for on-site wastewater disposal. If water in these clogged systems were contaminated by pathogens, it would pose a threat to human health. We isolated Stenotrophomonas maltophilia strain WR-C from a clogged septic tank system that consistently formed biofilms on sand grains, produced exopolysaccharides (EPS), and caused clogging in sand columns (33). S. maltophilia is a gram-negative, rod-shaped, and obligate aerobic bacterium with polar flagella in the ␥-␤ subdivision of Proteobacteria (3,14). It is found in various environments and recently has emerged as an important human pathogen. Very little is known about the mechanisms of biofilm formation by S. maltophilia. It has been shown to adhere to HEp-2 cells as well as abiotic surfaces, such as plastic, glass, and Teflon (7-10, 16).To identify genes that are involved in biofilm formation by S. maltophilia WR-C, about 4,500 transposon mutants generated with the EZ::TN Ͻ R6K␥ori/KAN-2 Ͼ Tnp transposome (Epicenter, Madison, Wis.) were screened for defects in biofilm formation in 96-well polystyrene plates (Becton-Dickinson Labware, Franklin Lakes, N.J.) by using a modified microtiter plate assay (11,29). Briefly, wells containing 200 l Trypticase soy (TS) broth were inoculated with overnight cultures and incubated at 30°C, 50 rpm for 2 days. Biofilm cells were stained with 0.1% crystal violet and washed, the stain remaining in the cells was solubilized with 70% ethanol, and the optical density at 590 nm was determined. Three mutants, TPH7, TPH11, and TPH13, whose growth was similar to that of the wild type but which were deficient in biofilm formation, were selected for further characterization.The transposon flanking regions were rescued by "rescue cloning" as described by the manufacturer and sequenced by using the primers KAN-2 FP-1 and R6KAN-2 RP-1 (Table 1). The transposon-inserted genes are homologous to three genes involved in the biosynthesis of nucleotide sugar precursors of lipopolysaccharide (LPS) and EPS in Xanthomonas campestris pv. campestris ATCC 33913 (GenBank accession no. AE008922) (6). The genes are rmlC (for TPH7, 74% identity), rmlA (for TPH11, 78% identity), and xanB (for TPH13, 80% identity), which are located in the rml and xan operons of X. campestris pv. campestris (19,20). As no genome sequence is available and the gene cluster involved in LPS/EPS biosynthesis has not been reported for S. maltophilia, the DNA segments flanking the transposon in TPH7, TPH11, and TPH13 were sequenced. The complete sequences of the rmlBACD and xanAB operons and their flanking genes were deter...

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p‐Aminobenzoic acid inhibits the growth of soybean pathogen Xanthomonas axonopodis pv. glycines by altering outer membrane integrity

Jiang

Liu

Shi

et al. 2023

Pest Management Science

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BACKGROUNDp‐Aminobenzoic acid (pABA) is an environmentally friendly bioactive metabolite synthesized by Lysobacter antibioticus. This compound showed an unusual antifungal mode of action based on cytokinesis inhibition. However, the potential antibacterial properties of pABA remain unexplored.RESULTSIn this study, pABA showed antibacterial activity against Gram‐negative bacteria. This metabolite inhibited growth (EC50 = 4.02 mM), and reduced swimming motility, extracellular protease activity, and biofilm formation in the soybean pathogen Xanthomonas axonopodis pv. glycines (Xag). Although pABA was previously reported to inhibit fungal cell division, no apparent effect was observed on Xag cell division genes. Instead, pABA reduced the expression of various membrane integrity‐related genes, such as cirA, czcA, czcB, emrE, and tolC. Consistently, scanning electron microscopy observations revealed that pABA caused major alternations in Xag morphology and blocked the formation of bacterial consortiums. In addition, pABA reduced the content and profile of outer membrane proteins and lipopolysaccharides in Xag, which may explain the observed effects. Preventive and curative applications of 10 mM pABA reduced Xag symptoms in soybean plants by 52.1% and 75.2%, respectively.CONCLUSIONSThe antibacterial properties of pABA were studied for the first time, revealing new insights into its potential application for the management of bacterial pathogens. Although pABA was previously reported to show an antifungal mode of action based on cytokinesis inhibition, this compound inhibited Xag growth by altering the outer membrane's integrity. © 2023 Society of Chemical Industry.

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Role of Phosphoglucomutase of Stenotrophomonas maltophilia in Lipopolysaccharide Biosynthesis, Virulence, and Antibiotic Resistance

Cited by 81 publications

References 66 publications

Phosphoglucomutase ofYersinia pestisIs Required for Autoaggregation and Polymyxin B Resistance

Phosphoglucomutase ofYersinia pestisIs Required for Autoaggregation and Polymyxin B Resistance

Differential Biofilm Formation and Motility Associated with Lipopolysaccharide/Exopolysaccharide-Coupled Biosynthetic Genes inStenotrophomonas maltophilia

p‐Aminobenzoic acid inhibits the growth of soybean pathogen Xanthomonas axonopodis pv. glycines by altering outer membrane integrity

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