ArticleJournal of bacteriology2013
Characterization of the interaction between the chlamydial adhesin OmcB and the human host cell.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- The distinct trimeric structure of the immunodominant chlamydial antigen Major Outer Membrane Protein.Nature communications · 2026Article
- Elevated vaginal heparan sulfate correlates with impaired neutrophil killing ofInfection and immunity · 2026Article
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- Pathogenicity and virulence ofVirulence · 2025Review
- Genome-wide identification of modulators of Chlamydia trachomatis parasitophorous vacuole stability highlights an important role for sphingolipid supply.PLoS biology · 2025Article
- 3-O Sulfated Heparan Sulfate (G2) Peptide Ligand Impairs the Infectivity ofBiomolecules · 2025Article
- Sulfated Glycosaminoglycans as Inhibitors for Chlamydia Infections: Molecular Weight and Sulfation Dependence.Macromolecular bioscience · 2025Article
- The secreted host-cell protein clusterin interacts with PmpD and promotesFrontiers in cellular and infection microbiology · 2024Article
- Virulence Protein Pgp3 Is Insufficient To Mediate Plasmid-Dependent Infectivity of Chlamydia trachomatis.Infection and immunity · 2023Article
- Plasmid-mediated virulence inFrontiers in cellular and infection microbiology · 2023Review
- Pmp Repertoires Influence the Different Infectious Potential of Avian and MammalianFrontiers in microbiology · 2021Article
- Pathogenic Puppetry: Manipulation of the Host Actin Cytoskeleton byInternational journal of molecular sciences · 2019Review
- Performance of Chlamydia trachomatis OmcB Enzyme-Linked Immunosorbent Assay in Serodiagnosis of Chlamydia trachomatis Infection in Women.Journal of clinical microbiology · 2018Article
- Virulence-related comparative transcriptomics of infectious and non-infectious chlamydial particles.BMC genomics · 2018Article
- Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development.Frontiers in pharmacology · 2018Review
- The novel chlamydial adhesin CPn0473 mediates the lipid raft-dependent uptake of Chlamydia pneumoniae.Cellular microbiology · 2016Article
- Systematic protein interactome analysis of glycosaminoglycans revealed YcbS as a novel bacterial virulence factor.Scientific reports · 2016Article
- Article
- Surface Proteoglycans as Mediators in Bacterial Pathogens Infections.Frontiers in microbiology · 2016Review
- 2-O-Sulfated Domains in Syndecan-1 Heparan Sulfate Inhibit Neutrophil Cathelicidin and Promote Staphylococcus aureus Corneal Infection.The Journal of biological chemistry · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In a previous study, we reported that the OmcB protein from Chlamydia pneumoniae mediates adhesion of the infectious elementary body to human HEp-2 cells by interacting with heparin/heparan sulfate-like glycosaminoglycans (GAGs) via basic amino acids located in the first of a pair of XBBXBX heparin-binding motifs (K. Moelleken and J. H. Hegemann, Mol. Microbiol. 67:403-419, 2008). In the present study, we show that the basic amino acid at position 57 (arginine) in the first XBBXBX motif, the basic amino acid at position 61 (arginine) in the second motif, and another amino acid (lysine 69) C terminal to it play key roles in the interaction. In addition, we show that discrimination between heparin-dependent and -independent adhesion by C. trachomatis OmcBs is entirely dependent on three variable amino acids in the so-called variable domain C terminal to the conserved XBBXBX motif. Here, the predicted conformational change in the secondary structure induced by the proline at position 66 seems to be crucial for heparin recognition. Finally, we performed neutralization experiments using different anti-heparan sulfate antibodies to gain insight into the nature of the GAGs recognized by OmcB. The results suggest that C. trachomatis serovar L2 OmcB interacts with 6-O-sulfated domains of heparan sulfate, while C. pneumoniae OmcB apparently interacts with domains of heparan sulfate harboring a diverse subset of O-sulfations.
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