ArticleMolecular microbiology2008
Contact-dependent growth inhibition requires the essential outer membrane protein BamA (YaeT) as the receptor and the inner membrane transport protein AcrB.
Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers.
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Who cites it
135 citing papers in PubMed, 187 citations in OpenAlex.
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- C-terminal domain of the filamentous hemagglutinin FhaB is crucial for interaction ofbioRxiv : the preprint server for biology · 2026Article
- Elongation Factor Tu Acts as a Chaperone to Activate an Antibacterial RNase Toxin.Molecular microbiology · 2026Article
- A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The yxiD gene from Bacillus subtilis 6633 encodes a polymorphic toxin with tRNase activity and is neutralized by the cognate immunity protein YxxD.Nucleic acids research · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- An Rcs Stress-Based High-Throughput Screen Reveals Novel Gyrase Inhibitors as Indirect Inducers of Cell Envelope Stress in Gram-Negative Bacteria.ACS infectious diseases · 2025Article
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- The Competitive Edge: T6SS-Mediated Interference Competition byMicroorganisms · 2025Review
- Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition.Nature communications · 2025Article
- Permeabilisation of the Outer Membrane of Escherichia coli for Enhanced Transport of Complex Molecules.Microbial biotechnology · 2025Article
- Contact-dependent growth inhibition (CDI) systems deploy a large family of polymorphic ionophoric toxins for inter-bacterial competition.PLoS genetics · 2024Article
- Autoproteolytic mechanism of CdiA toxin release reconstitutedJournal of bacteriology · 2024Article
- Mechanisms of bacterial immunity, protection, and survival during interbacterial warfare.Cell host & microbe · 2024Review
- Site-Specific Photocrosslinking to Investigate Toxin Delivery Mediated by the Bacterial β-Barrel Assembly Machine.Methods in molecular biology (Clifton, N.J.) · 2024Article
- In Silico Analysis and Immune Response of YaeT Protein Against Riemerella anatipestifer in Ducks.Applied biochemistry and biotechnology · 2023Article
- TamAB is regulated by PhoPQ and functions in outer membrane homeostasis duringJournal of bacteriology · 2023Article
- Article
- Mechanism of outer membrane destabilization by global reduction of protein content.Nature communications · 2023Article
- Drug resistance and physiological roles of RND multidrug efflux pumps inMicrobiology (Reading, England) · 2023Article
75 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
Contact-dependent growth inhibition (CDI) is a phenomenon by which bacterial cell growth is regulated by direct cell-to-cell contact via the CdiA/CdiB two-partner secretion system. Characterization of mutants resistant to CDI allowed us to identify BamA (YaeT) as the outer membrane receptor for CDI and AcrB as a potential downstream target. Notably, both BamA and AcrB are part of distinct multi-component machines. The Bam machine assembles outer membrane beta-barrel proteins into the outer membrane and the Acr machine exports small molecules into the extracellular milieu. We discovered that a mutation that reduces expression of BamA decreased binding of CDI+ inhibitor cells, measured by flow cytometry with fluorescently labelled bacteria. In addition, alpha-BamA antibodies, which recognized extracellular epitopes of BamA based on immunofluorescence, specifically blocked inhibitor-target cells binding and CDI. A second class of CDI-resistant mutants identified carried null mutations in the acrB gene. AcrB is an inner membrane component of a multidrug efflux pump that normally forms a cell envelope-spanning complex with the membrane fusion protein AcrA and the outer membrane protein TolC. Strikingly, the requirement for the BamA and AcrB proteins in CDI is independent of their multi-component machines, and thus their role in the CDI pathway may reflect novel, import-related functions.
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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.