ArticleMolecular microbiology2011
DsbA2 (27 kDa Com1-like protein) of Legionella pneumophila catalyses extracytoplasmic disulphide-bond formation in proteins including the Dot/Icm type IV secretion system.
Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Type IV secretion systems: from structures to mechanisms.The EMBO journal · 2025Review
- The Passage of Chaperonins to Extracellular Locations inBiomolecules · 2025Article
- Analysis of the Brucella suis Twin Arginine Translocation System and Its Substrates Shows That It Is Essential for Viability.Infection and immunity · 2023Article
- Role ofFrontiers in microbiology · 2023Review
- Knowledge to Predict Pathogens:Microorganisms · 2022Review
- Identification of Immunogenic Linear B-Cell Epitopes inPathogens (Basel, Switzerland) · 2021Article
- Evaluation of the Diagnostic Potential of RecombinantMicroorganisms · 2020Article
- Disulfide bond formation in prokaryotes.Nature microbiology · 2018Review
- Dual Role for DsbA in Attacking and Targeted Bacterial Cells during Type VI Secretion System-Mediated Competition.Cell reports · 2018Article
- Article
- Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies.Applied microbiology and biotechnology · 2017Review
- Components of the type six secretion system are substrates of Francisella tularensis Schu S4 DsbA-like FipB protein.Virulence · 2016Article
- Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231).Frontiers in microbiology · 2016Article
- Life Stage-specific Proteomes of Legionella pneumophila Reveal a Highly Differential Abundance of Virulence-associated Dot/Icm effectors.Molecular & cellular proteomics : MCP · 2016Article
- Legionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerization.Molecular microbiology · 2015Article
- Identification of disulfide bond isomerase substrates reveals bacterial virulence factors.Molecular microbiology · 2014Article
- The many forms of a pleomorphic bacterial pathogen-the developmental network of Legionella pneumophila.Frontiers in microbiology · 2014Review
- Article
- Review
- Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activity.Journal of bacteriology · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
In Gram-negative bacteria, thiol oxidoreductases catalyse the formation of disulphide bonds (DSB) in extracytoplasmic proteins. In this study, we sought to identify DSB-forming proteins required for assembly of macromolecular structures in Legionella pneumophila. Here we describe two DSB-forming proteins, one annotated as dsbA1 and the other annotated as a 27 kDa outer membrane protein similar to Com1 of Coxiella burnetii, which we designate as dsbA2. Both proteins are predicted to be periplasmic, and while dsbA1 mutants were readily isolated and without phenotype, dsbA2 mutants were not obtained. To advance studies of DsbA2, a cis-proline residue at position 198 was replaced with threonine that enables formation of stable disulphide-bond complexes with substrate proteins. Expression of DsbA2 P198T mutant protein from an inducible promoter produced dominant-negative effects on DsbA2 function that resulted in loss of infectivity for amoeba and HeLa cells and loss of Dot/Icm T4SS-mediated contact haemolysis of erythrocytes. Analysis of captured DsbA2 P198T-substrate complexes from L. pneumophila by mass spectrometry identified periplasmic and outer membrane proteins that included components of the Dot/Icm T4SS. More broadly, our studies establish a DSB oxidoreductase function for the Com1 lineage of DsbA2-like proteins which appear to be conserved among those bacteria also expressing T4SS.
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