ArticleNature communications2021
The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 97 citations in OpenAlex.
- Article
- Tangled Up in Fibers: How a Multidomain Lytic Polysaccharide Monooxygenase Binds Its Chitin Substrate.ACS applied materials & interfaces · 2026Article
- Assessment and functional genomic investigation of methane and nitrogen metabolizing pathways in Pseudomonas aeruginosa strain AAK/M5.World journal of microbiology & biotechnology · 2026Article
- Redox robustness drives LPMO evolution.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Discovery of a Copper-Binding Carbohydrate-Binding Module Regulating the Activity of Lytic Polysaccharide Monooxygenases.Journal of the American Chemical Society · 2025Article
- Pre-adsorption of serum albumin on biomaterial surfaces modulates bacteria-surface interactions and alters bacterial physiological responses.Materials today. Bio · 2025Article
- N-acetyl-glucosamine primes Pseudomonas aeruginosa for virulence through a type IV pili/cAMP-mediated morphology transition.Nature communications · 2025Article
- Identification and characterization of two AA9 lytic polysaccharide monooxygenases isolated from the enzymatic arsenal in Phanerochaete chrysosporium.Bioresources and bioprocessing · 2025Article
- The Egh16-like virulence factor TrsA of the nematode-trapping fungus Arthrobotrys flagrans facilitates intrusion into its host Caenorhabditis elegans.PLoS pathogens · 2025Article
- Structure-Function Analysis of an Understudied Type of LPMO with Unique Redox Properties and Substrate Specificity.ACS catalysis · 2025Article
- Functional variation among LPMOs revealed by the inhibitory effects of cyanide and buffer ions.FEBS letters · 2025Article
- AlphaFold prediction of structural ensembles of disordered proteins.Nature communications · 2025Article
- Massive Gene Loss in the Fungus Sporothrix epigloea Accompanied a Shift to Life in a Glucuronoxylomannan-based Gel Matrix.Genome biology and evolution · 2025Article
- Mutations in mexT bypass the stringent response dependency of virulence in Pseudomonas aeruginosa.Cell reports · 2025Article
- Exploring roles of the chitinase ChiC in modulatingMicrobiology spectrum · 2024Article
- Article
- Mimicking the Reactivity of LPMOs with a Mononuclear Cu Complex.European journal of inorganic chemistry · 2024Article
- Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO).Nature communications · 2024Article
- Structural dissection of two redox proteins from the shipworm symbiont Teredinibacter turnerae.IUCrJ · 2024Article
- Inhibition ofAntimicrobial agents and chemotherapy · 2024Article
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Authors and funding
20 authors at 8 institutions in 4 countries.
Funding
Abstract
The recently discovered lytic polysaccharide monooxygenases (LPMOs), which cleave polysaccharides by oxidation, have been associated with bacterial virulence, but supporting functional data is scarce. Here we show that CbpD, the LPMO of Pseudomonas aeruginosa, is a chitin-oxidizing virulence factor that promotes survival of the bacterium in human blood. The catalytic activity of CbpD was promoted by azurin and pyocyanin, two redox-active virulence factors also secreted by P. aeruginosa. Homology modeling, molecular dynamics simulations, and small angle X-ray scattering indicated that CbpD is a monomeric tri-modular enzyme with flexible linkers. Deletion of cbpD rendered P. aeruginosa unable to establish a lethal systemic infection, associated with enhanced bacterial clearance in vivo. CbpD-dependent survival of the wild-type bacterium was not attributable to dampening of pro-inflammatory responses by CbpD ex vivo or in vivo. Rather, we found that CbpD attenuates the terminal complement cascade in human serum. Studies with an active site mutant of CbpD indicated that catalytic activity is crucial for virulence function. Finally, profiling of the bacterial and splenic proteomes showed that the lack of this single enzyme resulted in substantial re-organization of the bacterial and host proteomes. LPMOs similar to CbpD occur in other pathogens and may have similar immune evasive functions.
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