ArticleMicrobiologyOpen2019
The advance of assembly of exopolysaccharide Psl biosynthesis machinery in Pseudomonas aeruginosa.
Article in MicrobiologyOpen, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Advances in bacterial synthesis pathways of bioflocculants and their applications in mine wastewater treatment.World journal of microbiology & biotechnology · 2026Review
- A choline-sensing regulator coordinates metabolic adaptation and pathogenesis inScience advances · 2025Article
- Biofilm and Outer Membrane Vesicle Formation in ESKAPE Gram-Negative Bacteria: A Comprehensive Review.International journal of molecular sciences · 2025Review
- Strain-specific variation in the complement resistome ofInfection and immunity · 2025Article
- A biofilm-tropiceLife · 2025Article
- ARTP mutagenesis for genome-wide identification of genes important for biofilm regulation in spoilage bacteriumApplied and environmental microbiology · 2025Article
- Biofilm formation: mechanistic insights and therapeutic targets.Molecular biomedicine · 2023Review
- Pseudomonas aeruginosa biofilm exopolysaccharides: assembly, function, and degradation.FEMS microbiology reviews · 2023Review
- Mutation of putative glycosyl transferases PslC and PslI confers susceptibility to antibiotics and leads to drastic reduction in biofilm formation inMicrobiology (Reading, England) · 2023Article
- Next-generation proteomics for quantitative Jumbophage-bacteria interaction mapping.Nature communications · 2023Article
- State of Innovation in Alginate-Based Materials.Marine drugs · 2023Review
- Role of Exopolysaccharides ofPolymers · 2022Review
- Intracellular glycosyl hydrolase PslG shapes bacterial cell fate, signaling, and the biofilm development ofeLife · 2022Article
- A Shaving Proteomic Approach to Unveil Surface Proteins Modulation of Multi-Drug ResistantFrontiers in medicine · 2022Article
- Effect of Polyhexamethylene Biguanide in Combination with Undecylenamidopropyl Betaine or PslG on Biofilm Clearance.International journal of molecular sciences · 2021Article
- Genomic Features of a Food-DerivedInternational journal of molecular sciences · 2020Article
- Untethering and Degradation of the Polysaccharide Matrix Are Essential Steps in the Dispersion Response ofJournal of bacteriology · 2020Article
- The advance of assembly of exopolysaccharide Psl biosynthesis machinery in Pseudomonas aeruginosa.MicrobiologyOpen · 2019Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biofilms are microbial communities embedded in extracellular matrix. Exopolysaccharide Psl (ePsl) is a key biofilm matrix component that initiates attachment, maintains biofilms architecture, and protects bacteria within biofilms of Pseudomonas aeruginosa, an opportunistic pathogen. There are at least 12 Psl proteins involved in the biosynthesis of this exopolysaccharide. However, it remains unclear about the function of each Psl protein and how these proteins work together during the biosynthesis of ePsl. PslG has been characterized as a degrader of ePsl in extracellular or periplasm and PslD is predicted to be a transporter. In this study, we found that PslG and its glycoside hydrolytic activity were also involved in the biosynthesis of ePsl. PslG localized mainly in the inner membrane and some in the periplasm. The inner membrane association of PslG was critical for the biosynthesis of ePsl. The expression of PslA, PslD, and PslE helped PslG remain in the inner membrane. The bacterial two-hybrid results suggested that PslE could interacted with either PslA, PslD, or PslG. The strongest interaction was found between PslE and PslD. Consistently, PslD was disabled to localize on the outer membrane in the ΔpslE strain, suggesting that the PslE-PslD interaction affected the localization of PslD. Our results shed light on the assembly of ePsl biosynthesis machinery and suggested that the membrane-associated PslG was a part of ePsl biosynthesis proteins complex.
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