ArticleMicrobiology (Reading, England)2015
The group I pilin glycan affects type IVa pilus hydrophobicity and twitching motility in Pseudomonas aeruginosa 1244.
Article in Microbiology (Reading, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- The O-glycan is essential for the induction of protective antibodies against lethal infection by flagella A-bearingInfection and immunity · 2024Article
- Type IV Pilus-Mediated Inhibition ofMicrobiology spectrum · 2023Article
- Metabolic Glycan Labeling-Based Screen to Identify Bacterial Glycosylation Genes.ACS infectious diseases · 2020Article
- Metabolic inhibitors of bacterial glycan biosynthesis.Chemical science · 2020Article
- The structure of PilA fromThe Journal of biological chemistry · 2019Article
- Pseudomonas aeruginosa defends against phages through type IV pilus glycosylation.Nature microbiology · 2018Article
- Structural Diversity in the Type IV Pili of Multidrug-resistant Acinetobacter.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The group I pilin category is the most common type of type IVa pilus produced by Pseudomonas aeruginosa. The lateral surfaces of these pili are characterized by the presence of closely spaced, covalently attached O-antigen repeating units. The current work was conducted to investigate the pilin glycan's effect on pilus solubility and function. Culture supernatant fluids containing fully, partially and non-glycosylated P. aeruginosa group I pili were tested for solubility in the presence of ammonium sulfate. These results showed that while pili expressing three or four sugars were highly soluble under all conditions, those with fewer than three were insoluble under the lowest salt concentrations tested. A representative of the P. aeruginosa group II pili also showed low solubility when assayed under these same conditions. Reduced solubility suggested an increased pilus surface hydrophobicity, which was supported by protein modelling. While having no effect on the WT strain, an ionic strength found at many host infection sites inhibited surface and subsurface twitching motility of strain 1244G7, an isogenic mutant unable to glycosylate pilin. This effect was reversed by mutant complementation. Twitching motility of P. aeruginosa strain PA103, which produces group II pili, was also inhibited by ionic strengths which influenced the mutant 1244 strain. We suggest that the group I pilin glycan may, therefore, be beneficial to this organism specifically for optimal pilus functioning at the many host disease sites with ionic strengths comparable to those tested here.
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