ArticleMolecular microbiology2020
A type VI secretion system delivers a cell wall amidase to target bacterial competitors.
Article in Molecular microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
The trial behind it
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- A dual-action bacteriophage protein Ped1 degrades DNA and blocks replication in Pseudomonas aeruginosa.The EMBO journal · 2026Article
- Genome-Wide In Silico Analysis of the Type VI Secretion System (T6SS) Within the Morganella Genus.MicrobiologyOpen · 2026Article
- A nonenzymatic effector disruptsProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Identification of type VI secretion system effector-immunity pairs using structural bioinformatics.Molecular systems biology · 2024Article
- T6SS: A Key to Pseudomonas's Success in Biocontrol?Microorganisms · 2023Review
- Amber-codon suppression for spatial localization and in vivo photoaffinity capture of the interactome of the Pseudomonas aeruginosa rare lipoprotein A lytic transglycosylase.Protein science : a publication of the Protein Society · 2023Article
- The T6SS-Dependent Effector Re78 ofBiology · 2023Article
- Effectiveness of Pseudomonas aeruginosa type VI secretion system relies on toxin potency and type IV pili-dependent interaction.PLoS pathogens · 2023Article
- YgfB increases β-lactam resistance in Pseudomonas aeruginosa by counteracting AlpA-mediated ampDh3 expression.Communications biology · 2023Article
- Bacterial type VI secretion system (T6SS): an evolved molecular weapon with diverse functionality.Biotechnology letters · 2023Review
- Role of Enzymatic Activity in the Biological Cost Associated with the Production of AmpC β-Lactamases in Pseudomonas aeruginosa.Microbiology spectrum · 2022Article
- Antibacterial contact-dependent proteins secreted by Gram-negative cystic fibrosis respiratory pathogens.Trends in microbiology · 2022Review
- Pseudomonas aeruginosa Alters Peptidoglycan Composition under Nutrient Conditions Resembling Cystic Fibrosis Lung Infections.mSystems · 2022Article
- Pseudomonas aeruginosa: pathogenesis, virulence factors, antibiotic resistance, interaction with host, technology advances and emerging therapeutics.Signal transduction and targeted therapy · 2022Review
- ECF Sigma Factor HxuI Is Critical forMicrobiology spectrum · 2022Article
- Antimicrobial Weapons of Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022Article
- The ecological impact of a bacterial weapon: microbial interactions and the Type VI secretion system.FEMS microbiology reviews · 2021Article
- Targeting the Achilles' Heel of Bacteria: Different Mechanisms To Break Down the Peptidoglycan Cell Wall during Bacterial Warfare.Journal of bacteriology · 2021Review
- Contact-independent killing mediated by a T6SS effector with intrinsic cell-entry properties.Nature communications · 2021Article
- Impacts of Ser/Thr Protein Kinase Stk1 on the Proteome, Twitching Motility, and Competitive Advantage inFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
The human pathogen Pseudomonas aeruginosa harbors three paralogous zinc proteases annotated as AmpD, AmpDh2, and AmpDh3, which turn over the cell wall and cell wall-derived muropeptides. AmpD is cytoplasmic and plays a role in the recycling of cell wall muropeptides, with a link to antibiotic resistance. AmpDh2 is a periplasmic soluble enzyme with the former anchored to the inner leaflet of the outer membrane. We document, herein, that the type VI secretion system locus II (H2-T6SS) of P. aeruginosa delivers AmpDh3 (but not AmpD or AmpDh2) to the periplasm of a prey bacterium upon contact. AmpDh3 hydrolyzes the cell wall peptidoglycan of the prey bacterium, which leads to its killing, thereby providing a growth advantage for P. aeruginosa in bacterial competition. We also document that the periplasmic protein PA0808, heretofore of unknown function, affords self-protection from lysis by AmpDh3. Cognates of the AmpDh3-PA0808 pair are widely distributed across Gram-negative bacteria. Taken together, these findings underscore the importance of their function as an evolutionary advantage and that of the H2-T6SS as the means for the manifestation of the effect.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.