ArticlePloS one2015
Biochemical Analysis of CagE: A VirB4 Homologue of Helicobacter pylori Cag-T4SS.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- Article
- The Effect ofPathogens (Basel, Switzerland) · 2025Article
- Roles of the components of theFuture microbiology · 2024Review
- A Proposal for a Consolidated Structural Model of the CagY Protein ofInternational journal of molecular sciences · 2023Article
- Characterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICEJournal of bacteriology · 2023Article
- Immunoinformatic prediction of potential immunodominant epitopes from cagW in order to investigate protection against Helicobacter pylori infection based on experimental consequences.Functional & integrative genomics · 2023Article
- Effects ofFrontiers in immunology · 2023Review
- Hesperetin Inhibits Expression of Virulence Factors and Growth ofInternational journal of molecular sciences · 2021Article
- Engagement of CEACAM1 byMicroorganisms · 2021Article
- Biofilm Formation as a Complex Result of Virulence and Adaptive Responses ofPathogens (Basel, Switzerland) · 2020Review
- Role of amoebae for survival and recovery of 'non-culturable' Helicobacter pylori cells in aquatic environments.FEMS microbiology ecology · 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
- Bacterial Energetic Requirements for Helicobacter pylori Cag Type IV Secretion System-Dependent Alterations in Gastric Epithelial Cells.Infection and immunity · 2020Article
- Defining theFrontiers in microbiology · 2020Article
- Comparative genome analysis ofMicrobial genomics · 2019Article
- Acid-regulated gene expression of Helicobacter pylori: Insight into acid protection and gastric colonization.Helicobacter · 2018Article
- Analyzing the role of CagV, a VirB8 homolog of the type IV secretion system ofFEBS open bio · 2017Article
- Determination ofMedical journal of the Islamic Republic of Iran · 2017Article
- Article
- 'Modulation of the enzymatic activities of replicative helicase (DnaB) by interaction with Hp0897: a possible mechanism for helicase loading in Helicobacter pylori'.Nucleic acids research · 2016Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Helicobacter pylori are among the most successful human pathogens that harbour a distinct genomic segment called cag Pathogenicity Island (cag-PAI). This genomic segment codes for a type IV secretion system (Cag-T4SS) related to the prototypical VirB/D4 system of Agrobacterium tumefaciens (Ag), a plant pathogen. Some of the components of Cag-T4SS share homology to that of VirB proteins including putative energy providing CagE (HP0544), the largest VirB4 homologue. In Ag, VirB4 is required for the assembly of the system, substrate translocation and pilus formation, however, very little is known about CagE. Here we have characterised the protein biochemically, genetically, and microscopically and report that CagE is an inner membrane associated active NTPase and has multiple interacting partners including the inner membrane proteins CagV and Cagβ. Through CagV it is connected to the outer membrane sub-complex proteins. Stability of CagE is not dependent on several of the cag-PAI proteins tested. However, localisation and stability of the pilus associated CagI, CagL and surface associated CagH are affected in its absence. Stability of the inner membrane associated energetic component Cagβ, a VirD4 homologue seems to be partially affected in its absence. Additionally, CagA failed to cross the membrane barriers in its absence and no IL-8 induction is observed under infection condition. These results thus suggest the importance of CagE in Cag-T4SS functions. In future it may help in deciphering the mechanism of substrate translocation by the system.
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