Novel Insights into E. coli’s Hexuronate Metabolism: KduI Facilitates the Conversion of Galacturonate and Glucuronate under Osmotic Stress Conditions

Rothe, M.; Alpert, Carl-Alfred; Loh, Gunnar; Blaut, Michaël

doi:10.1371/journal.pone.0056906

Cited by 28 publications

(16 citation statements)

References 43 publications

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“…These metabolic products have been shown to be generated intracellularly when exogenous sugars such as lactose are metabolized by E. coli [88]. These compounds are present intracellularly in numerous organs of animals, and these E. coli strains utilize cytoplasmic UDP-glucuronyltransferases for mucopolysaccharide biosynthesis [89].…”

Section: Resultsmentioning

confidence: 99%

Transport proteins promoting Escherichia coli pathogenesis

Tang

Saier

2014

Microbial Pathogenesis

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Escherichia coli is a genetically diverse species infecting hundreds of millions of people worldwide annually. We examined seven well-characterized E. coli pathogens causing urinary tract infections, gastroenteritis, pyelonephritis and haemorrhagic colitis. Their transport proteins were identified and compared with each other and a non-pathogenic E. coli K12 strain to identify transport proteins related to pathogenesis. Each pathogen possesses a unique set of protein secretion systems for export to the cell surface or for injecting effector proteins into host cells. Pathogens have increased numbers of iron siderophore receptors and ABC iron uptake transporters, but the numbers and types of low-affinity secondary iron carriers were uniform in all strains. The presence of outer membrane iron complex receptors and high-affinity ABC iron uptake systems correlated, suggesting co-evolution. Each pathovar encodes a different set of pore-forming toxins and virulence-related outer membrane proteins lacking in K12. Intracellular pathogens proved to have a characteristically distinctive set of nutrient uptake porters, different from those of extracellular pathogens. The results presented in this report provide information about transport systems relevant to various types of E. coli pathogenesis that can be exploited in future basic and applied studies.

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Section: Resultsmentioning

confidence: 99%

Transport proteins promoting Escherichia coli pathogenesis

Tang

Saier

2014

Microbial Pathogenesis

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“…). It is interesting to note that the island encodes a 4‐deoxy‐L‐threo‐5‐hexosulose‐uronate ketol‐isomerase (KduI) and a 2‐deoxy‐D‐gluconate 3‐dehydrogenase (KduD), which have recently been proposed as two enzymes of an alternative pathway for galacturonate degradation in E. coli (Rothe et al ., ), and which can process the unsaturated galacturonate that is produced by GH105 via the kdgF (PH505_dn00060) encoded enzyme (Hobbs et al ., ). Another pectin‐responsive protein of the genomic island is the KDPG aldolase (2‐dehydro‐3‐deoxy‐phosphogluconate aldolase), which catalyzes a late step in the biodegradation of pectin by converting 2‐dehydro‐3‐deoxy‐D‐gluconate 6‐phosphate (KDPG) into pyruvate and D‐glyceraldehyde 3‐phosphate.…”

Section: Discussionmentioning

confidence: 97%

Aquatic adaptation of a laterally acquired pectin degradation pathway in marine gammaproteobacteria

Hehemann

Truong

Unfried

et al. 2017

Environmental Microbiology

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Summary Mobile genomic islands distribute functional traits between microbes and habitats, yet it remains unclear how their proteins adapt to new environments. Here we used a comparative phylogenomic and proteomic approach to show that the marine bacterium Pseudoalteromonas haloplanktis ANT/505 acquired a genomic island with a functional pathway for pectin catabolism. Bioinformatics and biochemical experiments revealed that this pathway encodes a series of carbohydrate‐active enzymes including two multi‐modular pectate lyases, PelA and PelB. PelA is a large enzyme with a polysaccharide lyase family 1 (PL1) domain and a carbohydrate esterase family 8 domain, and PelB contains a PL1 domain and two carbohydrate‐binding domains of family 13. Comparative phylogenomic analyses indicate that the pathway was most likely acquired from terrestrial microbes, yet we observed multi‐modular orthologues only in marine bacteria. Proteomic experiments showed that P. haloplanktis ANT/505 secretes both pectate lyases into the environment in the presence of pectin. These multi‐modular enzymes may therefore represent a marine innovation that enhances physical interaction with pectins to reduce loss of substrate and enzymes by diffusion. Our results revealed that marine bacteria can catabolize pectin, and highlight enzyme fusion as a potential adaptation that may facilitate microbial consumption of polymeric substrates in aquatic environments.

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“…As a control, cells were treated with the Tris‐EDTA buffer without lysozyme. The OD 600 was measured over 11 h every 15 min, and final OD 600 was calculated as described previously (Rothe et al ., ). Briefly, OD 600 values were calculated to 1 cm path length according to the following formula: OD 600 (transformed) = OD 600/ 0.1069.…”

Section: Methodsmentioning

confidence: 99%

Mild gut inflammation modulates the proteome of intestinal Escherichia coli

Schumann

Alpert

Engst

et al. 2013

Environmental Microbiology

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Using interleukin 10-deficient (IL-10(-/-) ) and wild-type mice monoassociated with either the adherent-invasive Escherichia coli UNC or the probiotic E. coli Nissle, the effect of a mild intestinal inflammation on the bacterial proteome was studied. Within 8 weeks, IL-10(-/-) mice monoassociated with E. coli UNC exhibited an increased expression of several proinflammatory markers in caecal mucosa. Escherichia coli Nissle-associated IL-10(-/-) mice did not do so. As observed previously for E. coli from mice with acute colitis, glycolytic enzymes were downregulated in intestinal E. coli UNC from IL-10(-/-) mice. In addition, the inhibitor of vertebrate C-type lysozyme, Ivy, was upregulated on messenger RNA (mRNA) and protein level in E. coli Nissle from IL-10(-/-) mice compared with E. coli UNC from these mice. Higher expression of Ivy in E. coli Nissle correlated with an improved growth of this probiotic strain in the presence of lysozyme-ethylenediaminetetraacetic acid (EDTA). By overexpressing Ivy, we demonstrated that Ivy contributes to a higher lysozyme resistance of E. coli, supporting the role of Ivy as a potential fitness factor. However, deletion of Ivy did not alter the growth phenotype of E. coli Nissle in the presence of lysozyme-EDTA, suggesting the existence of additional lysozyme inhibitors that can take over the function of Ivy.

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Novel Insights into E. coli’s Hexuronate Metabolism: KduI Facilitates the Conversion of Galacturonate and Glucuronate under Osmotic Stress Conditions

Cited by 28 publications

References 43 publications

Transport proteins promoting Escherichia coli pathogenesis

Transport proteins promoting Escherichia coli pathogenesis

Aquatic adaptation of a laterally acquired pectin degradation pathway in marine gammaproteobacteria

Mild gut inflammation modulates the proteome of intestinal Escherichia coli

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