ArticleThe Biochemical journal2005
Deciphering the molecular bases of Mycobacterium tuberculosis binding to the lectin DC-SIGN reveals an underestimated complexity.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
51 citing papers in PubMed, 104 citations in OpenAlex.
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- Enhanced Glycosylation Caused by Overexpression of Rv1002c in a Recombinant BCG Promotes Immune Response and Protects againstVaccines · 2024Article
- Immune Response to the Recombinant Apa Protein from Mycobacterium tuberculosis Expressed in Streptomyces lividans After Intranasal Administration in Mice. Induction of Protective Response to Tubercle Bacillus Aerosols Exposure.Current microbiology · 2024Article
- Impact of Methylthioxylose Substituents on the Biological Activities of Lipomannan and Lipoarabinomannan inACS infectious diseases · 2024Article
- Nanoscale clustering of mycobacterial ligands and DC-SIGN host receptors are key determinants for pathogen recognition.Science advances · 2023Article
- Mycobacterial Adhesion: From Hydrophobic to Receptor-Ligand Interactions.Microorganisms · 2022Review
- Immunological hyporesponsiveness in tuberculosis: The role of mycobacterial glycolipids.Frontiers in immunology · 2022Review
- Generation of Liposomes to Study the Effect ofInternational journal of molecular sciences · 2021Article
- Innate Immune Pattern Recognition Receptors of Mycobacterium tuberculosis: Nature and Consequences for Pathogenesis of Tuberculosis.Advances in experimental medicine and biology · 2021Article
- Effect of Protein O-Mannosyltransferase (MSMEG_5447) onFrontiers in microbiology · 2021Article
- Evolution of Drug-ResistantFrontiers in microbiology · 2021Review
- Molecular Recognition in C-Type Lectins: The Cases of DC-SIGN, Langerin, MGL, and L-Sectin.Chembiochem : a European journal of chemical biology · 2020Review
- Potential Plasticity of the Mannoprotein Repertoire Associated toMolecules (Basel, Switzerland) · 2020Article
- Identification of Secreted O-Mannosylated Proteins From BCG and Characterization of Immunodominant Antigens BCG_0470 and BCG_0980.Frontiers in microbiology · 2020Article
- Molecular Insights into DC-SIGN Binding to Self-Antigens: The Interaction with the Blood Group A/B Antigens.ACS chemical biology · 2019Article
- Deciphering the molecular basis of mycobacteria and lipoglycan recognition by the C-type lectin Dectin-2.Scientific reports · 2018Article
- Mycobacterial cell wall biosynthesis: a multifaceted antibiotic target.Parasitology · 2018Review
- Insights into Interactions of Mycobacteria with the Host Innate Immune System from a Novel Array of Synthetic Mycobacterial Glycans.ACS chemical biology · 2017Article
- Protein O-mannosylation deficiency increases LprG-associated lipoarabinomannan release by Mycobacterium tuberculosis and enhances the TLR2-associated inflammatory response.Scientific reports · 2017Article
- Scrutiny of Mycobacterium tuberculosis 19 kDa antigen proteoforms provides new insights in the lipoglycoprotein biogenesis paradigm.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
15 authors at 5 institutions in 1 country.
Funding
Abstract
Interactions between dendritic cells and Mycobacterium tuberculosis, the aetiological agent of tuberculosis in humans, are thought to be central to anti-mycobacterial immunity. We have previously shown that M. tuberculosis binds to human monocyte-derived dendritic cells mostly through the C-type lectin DC-SIGN (dendritic-cell-specific intercellular molecule-3-grabbing non-integrin)/CD209, and we have suggested that DC-SIGN may discriminate between mycobacterial species through recognition of the mannose-capping residues on the lipoglycan lipoarabinomannan of the bacterial envelope. Here, using a variety of fast- and slow-growing Mycobacterium species, we provide further evidence that mycobacteria recognition by DC-SIGN may be restricted to species of the M. tuberculosis complex. Fine analyses of the lipoarabinomannan molecules purified from these species show that the structure and amount of these molecules alone cannot account for such a preferential recognition. We propose that M. tuberculosis recognition by DC-SIGN relies on both a potential difference of accessibility of lipoarabinomannan in its envelope and, more probably, on the binding of additional ligands, possibly including lipomannan, mannose-capped arabinomannan, as well as the mannosylated 19 kDa and 45 kDa [Apa (alanine/proline-rich antigen)] glycoproteins. Altogether, our results reveal that the molecular basis of M. tuberculosis binding to DC-SIGN is more complicated than previously thought and provides further insight into the mechanisms of M. tuberculosis recognition by the immune system.
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