ArticleJournal of bacteriology2008
Protein subassemblies of the Helicobacter pylori Cag type IV secretion system revealed by localization and interaction studies.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 125 citations in OpenAlex.
- Deciphering the initiation pathway of CagT4SS assembly by in vitro reconstitution of subcomplexes.Nature communications · 2026Article
- Unveiling a missing component of the atypical type IV secretion system required for natural transformation of Helicobacter pylori.PLoS pathogens · 2026Article
- Unveiling a missing component of the atypical type IV secretion system required for natural transformation ofbioRxiv : the preprint server for biology · 2026Article
- Species-specific components of theInfection and immunity · 2025Article
- Functional and intricate interaction network connectingmicroLife · 2025Article
- Roles of the components of theFuture microbiology · 2024Review
- Genetic diversity of Helicobacter pylori type IV secretion system cagI and cagN genes and their association with clinical diseases.Scientific reports · 2023Article
- Mechanism of regulation of the Helicobacter pylori Cagβ ATPase by CagZ.Nature communications · 2023Article
- How Long Will It Take to Launch an EffectiveInfection and drug resistance · 2023Review
- A symbiotic bacterium of Antarctic fish reveals environmental adaptability mechanisms and biosynthetic potential towards antibacterial and cytotoxic activities.Frontiers in microbiology · 2022Article
- Hesperetin Inhibits Expression of Virulence Factors and Growth ofInternational journal of molecular sciences · 2021Article
- Association ofCanadian journal of gastroenterology & hepatology · 2021Review
- Contribution of Heptose Metabolites and theFrontiers in immunology · 2021Article
- A novel mode of control of nickel uptake by a multifunctional metallochaperone.PLoS pathogens · 2021Article
- The RNase J-Based RNA Degradosome Is Compartmentalized in the Gastric Pathogen Helicobacter pylori.mBio · 2020Article
- Article
- Identification of Pathogenicity Island Genes Associated with Loss of Type IV Secretion Function during Murine Infection with Helicobacter pylori.Infection and immunity · 2020Article
- Effect of the cagW-based gene vaccine on the immunologic properties of BALB/c mouse: an efficient candidate for Helicobacter pylori DNA vaccine.Journal of nanobiotechnology · 2020Article
- Defining theFrontiers in microbiology · 2020Article
- Genetic Profiling ofPathogens (Basel, Switzerland) · 2019Article
6 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Type IV secretion systems are possibly the most versatile protein transport systems in gram-negative bacteria, with substrates ranging from small proteins to large nucleoprotein complexes. In many cases, such as the cag pathogenicity island of Helicobacter pylori, genes encoding components of a type IV secretion system have been identified due to their sequence similarities to prototypical systems such as the VirB system of Agrobacterium tumefaciens. The Cag type IV secretion system contains at least 14 essential apparatus components and several substrate translocation and auxiliary factors, but the functions of most components cannot be inferred from their sequences due to the lack of similarities. In this study, we have performed a comprehensive sequence analysis of all essential or auxiliary Cag components, and we have used antisera raised against a subset of components to determine their subcellular localization. The results suggest that the Cag system contains functional analogues to all VirB components except VirB5. Moreover, we have characterized mutual stabilization effects and performed a comprehensive yeast two-hybrid screening for potential protein-protein interactions. Immunoprecipitation studies resulted in identification of a secretion apparatus subassembly at the outer membrane. Combining these data, we provide a first low-resolution model of the Cag type IV secretion apparatus.
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