ArticleNature communications2022
Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- WGS reveals high-risk clones of Pseudomonas aeruginosa harbouring extensive antimicrobial and predicted anti-phage defense systems recovered from diabetic foot ulcer patients in Egypt.BMC microbiology · 2026Article
- "Molecular insights into the bactericidal toxin Tle1 of Pseudomonas aeruginosa: Interaction with VgrG, its adaptor, and its immunity protein".The Journal of biological chemistry · 2026Article
- Integron architecture and virulence-associated gene profiles in extensively drug-resistant high-riskFrontiers in microbiology · 2026Article
- Genome-Wide Identification and Expression Profiling of Glycosidases, Lipases, and Proteases from Invasive Asian Palm Weevil,Insects · 2025Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PldA, a phospholipase D (PLD) effector, catalyzes hydrolysis of the phosphodiester bonds of glycerophospholipids-the main component of cell membranes-and assists the invasion of the opportunistic pathogen Pseudomonas aeruginosa. As a cognate immunity protein, PA3488 can inhibit the activity of PldA to avoid self-toxicity. However, the precise inhibitory mechanism remains elusive. We determine the crystal structures of full-length and truncated PldA and the cryogenic electron microscopy structure of the PldA-PA3488 complex. Structural analysis reveals that there are different intermediates of PldA between the "open" and "closed" states of the catalytic pocket, accompanied by significant conformational changes in the "lid" region and the peripheral helical domain. Through structure-based mutational analysis, we identify the key residues responsible for the enzymatic activity of PldA. Together, these data provide an insight into the molecular mechanisms of PldA invasion and its neutralization by PA3488, aiding future design of PLD-targeted inhibitors and drugs.
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