ArticlePloS one2012
Differential contribution of the repeats to heparin binding of HBHA, a major adhesin of Mycobacterium tuberculosis.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- A Pilot Proteomics Analysis ofInternational journal of molecular sciences · 2026Article
- Synthesis of Heparan Sulfate Hexadecasaccharides and Their Molecular Interaction with Mycobacterial Heparin-Binding Hemagglutinin for the Detection ofJournal of the American Chemical Society · 2026Article
- Stopping Tuberculosis at the Gate: The Role ofVaccines · 2025Review
- The Flp type IV pilus operon ofFrontiers in cellular and infection microbiology · 2022Article
- Feature of Adhesins Produced by Human Clinical Isolates ofMicroorganisms · 2020Article
- The Heparin-Binding Hemagglutinin ofFrontiers in cellular and infection microbiology · 2020Article
- G-Quadruplex-Forming DNA Aptamers Inhibit the DNA-Binding Function of HupB and Mycobacterium tuberculosis Entry into Host Cells.Molecular therapy. Nucleic acids · 2018Article
- Association of Mycobacterium Proteins with Lipid Droplets.Journal of bacteriology · 2018Article
- Rv0613c/MSMEG_1285 Interacts with HBHA and Mediates Its Proper Cell-Surface Exposure in Mycobacteria.International journal of molecular sciences · 2018Article
- A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics.Protein science : a publication of the Protein Society · 2018Review
- Heparin-Binding Hemagglutinin Adhesin (HBHA) Is Involved in Intracytosolic Lipid Inclusions Formation in Mycobacteria.Frontiers in microbiology · 2018Article
- A study on the immune response induced by a DNA vaccine encoding Mtb32C-HBHA antigen ofIranian journal of basic medical sciences · 2017Article
- Heparin-binding Hemagglutinin ofFrontiers in cellular and infection microbiology · 2017Article
- The bacterial and host factors associated with extrapulmonary dissemination ofFrontiers in biology · 2015Article
- Human coronavirus NL63 utilizes heparan sulfate proteoglycans for attachment to target cells.Journal of virology · 2014Article
- Toward Understanding the Essence of Post-Translational Modifications for the Mycobacterium tuberculosis Immunoproteome.Frontiers in immunology · 2014Review
- Human immunodeficiency virus and heparan sulfate: from attachment to entry inhibition.Frontiers in immunology · 2013Review
- Novel feature of Mycobacterium avium subsp. paratuberculosis, highlighted by characterization of the heparin-binding hemagglutinin adhesin.Journal of bacteriology · 2013Article
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTuberculosis remains one of the most important causes of global mortality and morbidity, and the molecular mechanisms of the pathogenesis are still incompletely understood. Only few virulence factors of the causative agent Mycobacterium tuberculosis are known. One of them is the heparin-binding haemagglutinin (HBHA), an important adhesin for epithelial cells and an extrapulmonary dissemination factor. HBHA mediates mycobacterial adherence to epithelial cells via the interactions of its C-terminal, lysine rich repeat domain with sulfated glycoconjugates on the surface of epithelial cells. METHODOLOGY/PRINCIPAL
findingsUsing defined heparin sulfate (HS) analogs, we determined the minimal heparin fragment length for HBHA binding and structural adaptations of the HBHA heparin-binding domain (HBD) upon binding to heparin. The NMR studies show significant shifts of all residues in the HBD upon interaction with heparin, with stronger shifts in the last repeats compared to the upstream repeats, and indicated that the HS fragments with 14 sugar units cover the entire C-terminal lysine-rich domain of HBHA. The differential implication of the repeats is determined by the relative position of prolines and lysines within each repeat, and may contribute to binding specificity. GAG binding induces a non-homogeneous structural rearrangement in the HBD, with stabilization of a nascent α-helix only in the last penta-repeats. CONCLUSION/SIGNIFICANCE: Mycobacterial HBHA undergoes structural adaptation upon interaction with GAGs, which is likely involved in binding specificities of the adhesin, and mycobacterial pathogens may use HBD polymorphisms for host or organ specificity. Further studies will aim at decoding the complementarity between HBD repeats and HS sequence.
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