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Exploring roles of the chitinase ChiC in modulating Pseudomonas aeruginosa virulence phenotypes

ABSTRACT: Chitinases are ubiquitous enzymes involved in biomass degradation and chitin turnover in nature. Pseudomonas aeruginosa (PA), an opportunistic human pathogen, expresses ChiC, a secreted glycoside hydrolase 18 (GH18) family chitinase. Despite speculation about ChiC's role in PA disease pathogenesis, there is scant evidence supporting this hypothesis. Since PA cannot catabolize chitin, we investigated the potential function(s) of ChiC in PA pathophysiology

INSTRUMENT(S):

ORGANISM(S): Pseudomonas Aeruginosa Pao1 Bacteria

SUBMITTER: Per Kristian Edvardsen

LAB HEAD: Gustav Vaaje-Kolstad

PROVIDER: PXD048596 | Pride | 2024-04-30

REPOSITORIES: Pride

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			Action	DRS
	210826_KO_ctrl_1.d.zip	Other
	210826_KO_ctrl_2.d.zip	Other
	210826_KO_ctrl_3.d.zip	Other
	210826_KO_pig_mucin_1.d.zip	Other
	210826_KO_pig_mucin_2.d.zip	Other

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Exploring roles of the chitinase ChiC in modulating Pseudomonas aeruginosa virulence phenotypes

Project description:Chitinases are ubiquitous enzymes involved in biomass degradation and chitin turnover in nature. Pseudomonas aeruginosa (PA), an opportunistic human pathogen, expresses ChiC, a secreted glycoside hydrolase 18 (GH18) family chitinase. Despite speculation about ChiC's role in PA disease pathogenesis, there is scant evidence supporting this hypothesis. Since PA cannot catabolize chitin, we investigated the potential function(s) of ChiC in PA pathophysiology

2024-04-30 | PXD048320 | Pride

The fish pathogen Aliivibrio salmonicida LFI1238 can degrade and utilize chitin as a nutrient source despite major gene loss in the chitinolytic pathway

Project description:The marine bacterium Aliivibriosalmonicida (formerly Vibrio salmonicida) is the causative agent of cold water vibriosis, a disease that led to severe losses in Norwegian aquaculture during the 1980s. Genes encoding a glycoside hydrolase family 18 (GH18) chitinase and two lytic polysaccharide monooxygenases (LPMOs) containing chitin binding domains are encoded in the genome of this bacterium, indicating a chitin degrading capability. However, due to extensive gene decay, some parts of the chitinolytic pathways are believed to be dysfunctional. To investigate the chitinolytic abilities of the bacterium, we combined microbiological and biochemical experiments with proteomic analysis. The family GH18 chitinase was able to depolymerize - and -chitin, but its activity was up to 50-fold lower compared to other well-studied chitinases from Serratia marcescens and Cellvibrio japonicus. The two LPMOs showed activity on chitin, cleaving the substrate chains by oxidation. Cultivation experiments showed that Al. salmonicida was able to grow on and utilize the soluble building blocks of chitin; N-acetyl-D-glucosamine (GlcNAc) and chitobiose (GlcNAc2). Furthermore, cultivation and gene deletion studies revealed that the bacterium was able to degrade insoluble chitin, albeit at a slow rate, and that growth on this substrate was dependent on the GH18 chitinase, but to a lesser extent the LPMOs. Finally, expression of the GH18 chitinase and both LPMOs was detected by proteomic analysis of Al. salmonicida cultivated on chitin as the sole carbon source. In conclusion, our results show that Al. salmonicida LFI1238 can utilize chitin as source of nutrients and its ability depends on the GH18 chitinase.

2021-07-26 | PXD021397 | Pride

Expression profiling of Cellvibrio japonicus using either glucose or chitin

Project description:Understanding the strategies used by bacteria to degrade polysaccharides constitutes an invaluable tool for biotechnological applications Bacteria are major mediators of polysaccharide degradation in nature, however the complex mechanisms used to detect, degrade, and consume these substrates are not well understood, especially for recalcitrant polysaccharides such as chitin It has been previously shown that the model bacterial saprophyte Cellvibrio japonicus is able to catabolize chitin, but little is known about the enzymatic machinery underlying this capability Previous analyses of the C japonicus genome and proteome indicated the presence of four family 18 Glycoside Hydrolase (GH18) enzymes, and studies of the proteome indicated that all are involved in chitin utilization Using a combination of in vitro and in vivo approaches, we have studied the roles of these four chitinases in chitin bioconversion Genetic analyses showed that only the chi18D gene product is essential for the degradation of chitin substrates Biochemical characterization of the four enzymes showed functional differences and synergistic effects during chitin degradation, indicating non-redundant roles in the cell Transcriptomic studies revealed complex regulation of the chitin degradation machinery of C japonicus and confirmed the importance of CjChi18D and CjLPMO10A, a previously characterized chitin-active enzyme With this systems biology approach, we deciphered the physiological relevance of the GH18 enzymes for chitin degradation in C japonicus, and the combination of in vitro and in vivo approaches provided a comprehensive understanding of the initial stages of chitin degradation by this bacterium

2018-01-24 | GSE108935 | GEO

Epithelial regeneration is modulated by chitin and chitinase activity

Project description:Epithelial injury underlies fibrotic and inflammatory lung diseases during which regenerative responses become dysregulated or recurrently engaged. Although environmental exposures are risk factors for severe lung disease, specific drivers of persistent epithelial and immune dysfunction are poorly understood. Here we identify a feedback circuit triggered by chitin, a common component of airborne particulate matter, that impacts lung health and regeneration after epithelial injury. In mice, damage to epithelial cells results in loss of homeostatic lung chitinase activity and accumulation of environmental chitin substrates; these disturbances impair epithelial renewal and drive activation of group 2 innate lymphoid cells (ILC2s). ILC2s, in turn, restore chitinase activity by inducing acidic mammalian chitinase (AMCase) in regenerating epithelial cells, thereby promoting chitin degradation, epithelial differentiation, and inflammatory resolution. Mice lacking AMCase or ILC2s fail to clear airway chitin and exhibit exacerbated inflammation, impaired epithelial regeneration, and increased mortality following epithelial injury. These effects are ameliorated by chitinase replacement therapy or AMCase overexpression, demonstrating that chitin degradation is crucial for restoring lung homeostasis after perturbation. The ILC2-chitinase response circuit thus comprises a tissue adaptation to a widespread environmental constituent and may be a target for alleviating persistent post-injury lung epithelial and immune dysfunction.

2024-12-31 | GSE275319 | GEO

Epithelial regeneration is modulated by chitin and chitinase activity

2024-12-31 | GSE275075 | GEO

Chitin degradation machinery and secondary metabolite profiles in the marine bacterium Pseudoalteromonas rubra S4059

Project description:Genome mining of pigmented Pseudoalteromonas has revealed a large potential for production of bioactive compounds, both hydrolytic enzymes and secondary metabolites and the purpose of the present study was to explore this bioactivity potential in a potent antibiotic and enzyme producer, Pseudoalteromonas rubra strain S4059. Proteomic analyses indicated that a highly efficient chitin degradation machinery was present in the red-pigmented P. rubra S4059 when grown on chitin. Four GH18 chitinases and two GH20 hexosaminidases were significantly upregulated by chitin. GH19 chitinase which is not common in bacteria is consistently found in pigmented Pseudoalteromonas and in S4059 it was only detected when the bacterium was grown on chitin. To explore the possible role of GH19 in pigmented Pseudoalteromonas, we deleted the GH19 chitinase and compared a range of phenotypes in the mutant and wild type. Neither, the chitin degrading ability or the biofilm forming capacity was affected by GH19 deletion. In some Vibrionaceae, the secondary metabolome is significantly affected by growth on chitin as compared to simpler carbon sources. The secondary metabolites produced by S4059 and the GH19 mutant were xxx start by chitin/mannose – then the mutant. not altered by the absence of the gene, indicating that chitin utilization may not directly influence the production of secondary metabolites as has been observed in some Vibrionaceae. Metabolome analysis reveal that growth on chitin XX. In summary,

2021-03-11 | PXD023249 | Pride

Atlantic salmon gastric mucosa LC-MSMS

Project description:The Atlantic salmon (Salmo salar) genome contains 10 chitinase encoding genes, but little is known about the function of these chitinases. Three of the chitinase genes have previously been shown to be expressed in the stomach tissue of Atlantic salmon. In the current study we show that the protein products of these genes, the family 18 glycoside hydrolase (GH18) chitinases, Chia.3, Chia.4 and Chia.7 are secreted into the stomach mucosa and are amongst the most abundant proteins in this matrix.

2022-05-08 | PXD030291 | Pride

Genomic and proteomic study of Andreprevotia ripae isolated from an anthill reveals an extensive repertoire of chitinolytic enzymes

Project description:Chitin is an abundant natural polysaccharide that is hard to degrade because of its crystalline nature and because it is often found embedded in robust co-polymeric materials containing other polysaccharides, proteins and minerals. Thus, it is of interest to study the enzymatic machineries of highly specialized microbes found in chitin-rich environments. We describe a genomic and proteomic analysis of the chitinolytic machinery of Andreprevotia ripae, a Gram-negative bacterium that was isolated from an anthill. The genome of A. ripae encodes four secreted family GH19 chitinases of which two were detected, both being upregulated during growth on chitin. In addition, the genome encodes 25 secreted GH18 chitinases, of which 17 were detected and 12 were upregulated during growth on chitin. Finally, the single lytic polysaccharide monooxygenase (LPMO) of A. ripae, predicted to be chitin-active based on sequence characteristics and the presence of chitin-binding domains, was strongly upregulated during growth on chitin. Whereas 66 % of the 29 secreted chitinases contained two carbo¬hydrate-binding modules (CBMs) known for binding to chitin, this fraction was 93 % (13 out of 14) for the chitinases that were upregulated during growth on chitin, suggesting an important role for these CBMs. Next to demonstrating an unprecedentedly large multiplicity of upregulated chitinases, the present study also revealed several chitin-induced proteins that contain chitin-binding domains but lack a known catalytic function. These proteins are interesting targets for discovery of enzymes used by Nature to convert chitin-rich biomass.

2021-06-10 | PXD025087 | Pride