ArticleJournal of bacteriology2006
Characterization of the pilin ortholog of the Helicobacter pylori type IV cag pathogenicity apparatus, a surface-associated protein expressed during infection.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 62 citations in OpenAlex.
- Experimental Approaches to Visualize Effector Protein Translocation During Host-Pathogen Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Genomic diversity of mcr-carrying plasmids and the role of type IV secretion systems in IncI2 plasmids conjugation.Communications biology · 2025Article
- Functional and intricate interaction network connectingmicroLife · 2025Article
- Roles of the components of theFuture microbiology · 2024Review
- Acid-regulated gene expression of Helicobacter pylori: Insight into acid protection and gastric colonization.Helicobacter · 2018Article
- In Vivo Structures of the Helicobacter pylori cag Type IV Secretion System.Cell reports · 2018Article
- Systematic site-directed mutagenesis of the Helicobacter pylori CagL protein of the Cag type IV secretion system identifies novel functional domains.Scientific reports · 2016Article
- Composition, structure and function of the Helicobacter pylori cag pathogenicity island encoded type IV secretion system.Future microbiology · 2015Review
- Article
- Genes required for assembly of pili associated with the Helicobacter pylori cag type IV secretion system.Infection and immunity · 2014Article
- Structural and functional aspects of the Helicobacter pylori secretome.World journal of gastroenterology · 2014Review
- Cag type IV secretion system: CagI independent bacterial surface localization of CagA.PloS one · 2013Article
- In vivo expression of Helicobacter pylori virulence genes in patients with gastritis, ulcer, and gastric cancer.Infection and immunity · 2012Article
- Characterization of CagI in the cag pathogenicity island of Helicobacter pylori.Current microbiology · 2012Article
- Inhibitory effects of anthocyanins on secretion of Helicobacter pylori CagA and VacA toxins.International journal of medical sciences · 2012Article
- CagI is an essential component of the Helicobacter pylori Cag type IV secretion system and forms a complex with CagL.PloS one · 2012Article
- Alterations in Helicobacter pylori triggered by contact with gastric epithelial cells.Frontiers in cellular and infection microbiology · 2012Review
- Conserved transcriptional unit organization of the cag pathogenicity island among Helicobacter pylori strains.Frontiers in cellular and infection microbiology · 2012Article
- Molecular mechanisms of gastric epithelial cell adhesion and injection of CagA by Helicobacter pylori.Cell communication and signaling : CCS · 2011Article
- Helicobacter pylori exploits a unique repertoire of type IV secretion system components for pilus assembly at the bacteria-host cell interface.PLoS pathogens · 2011Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Helicobacter pylori cag pathogenicity island (cag PAI) encodes components of a type IV secretion system (T4SS) involved in host interaction and pathogenicity. Previously, seven cag PAI proteins were identified as homologs of Agrobacterium tumefaciens Vir proteins, which form a paradigm T4SS. The T pilus composed of the processed VirB2 pilin is an external structural part of the A. tumefaciens T4SS. In H. pylori, cag-dependent assembly of pili has not been observed so far, nor has a pilin (VirB2) ortholog been characterized. We have here identified, using a motif-based search, an H. pylori cag island protein (HP0546) that possesses sequence and predicted structural similarities to VirB2-like pilins of other T4SSs. The HP0546 protein displays interstrain variability in its terminal domains. HP0546 was expressed as a FLAG-tagged fusion protein in Escherichia coli, A. tumefaciens, and H. pylori and was detected as either two or three bands of different molecular masses in the insoluble fraction, indicating protein processing. As reported previously, isogenic H. pylori mutants in the putative cag pilin gene had reduced abilities to induce cag PAI-dependent interleukin-8 secretion in gastric epithelial cells. Fractionation analysis of H. pylori, using a specific antiserum raised against an N-terminal HP0546 peptide, showed that the protein is partially surface exposed and that its surface localization depended upon an intact cag system. By immunoelectron microscopy, HP0546 was localized in surface appendages, with surface exposure of an N-terminal epitope. Pronounced strain-to-strain variability of this predicted surface-exposed part of HP0546 indicates a strong selective pressure for variation in vivo.
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