ArticleThe Journal of biological chemistry2014
Glycerol monomycolate is a novel ligand for the human, but not mouse macrophage inducible C-type lectin, Mincle.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.
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Who cites it
32 citing papers in PubMed, 1 synthesis or guideline pooled it, 84 citations in OpenAlex.
- Using proteomics and metabolomics to identify therapeutic targets for senescence mediated cancer: genetic complementarity method.Frontiers in endocrinology · 2023Pooled it
- Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026Review
- A stable two-component cationic liposome platform for mRNA delivery induces CD8Journal of nanobiotechnology · 2026Article
- Vacuolar sterol β-glucosidase EGCrP2/Sgl1 deficiency in Cryptococcus neoformans: Dysfunctional autophagy and Mincle-dependent immune activation as targets of novel antifungal strategies.PLoS pathogens · 2025Article
- Review
- Article
- Effect of Mycolic Acids on Host Immunity and Lipid Metabolism.International journal of molecular sciences · 2023Review
- Characterisation of the bovine C-type lectin receptor Mincle and potential evidence for an endogenous ligand.Frontiers in immunology · 2023Article
- Vector and Host C-Type Lectin Receptor (CLR)-Fc Fusion Proteins as a Cross-Species Comparative Approach to Screen for CLR-Rift Valley Fever Virus Interactions.International journal of molecular sciences · 2022Article
- Immunological hyporesponsiveness in tuberculosis: The role of mycobacterial glycolipids.Frontiers in immunology · 2022Review
- Mycobacterial surface characters remodeled by growth conditions drive different tumor-infiltrating cells and systemic IFN-γ/IL-17 release in bladder cancer treatment.Oncoimmunology · 2022Article
- Medicinal chemistry of the myeloid C-type lectin receptors Mincle, Langerin, and DC-SIGN.RSC medicinal chemistry · 2021Review
- TREM2 is a receptor for non-glycosylated mycolic acids of mycobacteria that limits anti-mycobacterial macrophage activation.Nature communications · 2021Article
- Elevated macrophage-inducible C-type lectin expression in the synovial tissue of patients with rheumatoid arthritis.Central-European journal of immunology · 2021Article
- C-Type Lectins in Veterinary Species: Recent Advancements and Applications.International journal of molecular sciences · 2020Review
- Expression and regulation of macrophage-inducible C-type lectin in human synovial macrophages.Central-European journal of immunology · 2020Article
- Synthesis of a Di-Mycoloyl Tri-Arabinofuranosyl Glycerol Fragment of the Mycobacterial Cell Wall, Based on Synthetic Mycolic Acids.Molecules (Basel, Switzerland) · 2019Article
- Species-Specific Structural Requirements of Alpha-Branched Trehalose Diester Mincle Agonists.Frontiers in immunology · 2019Article
- Rational Design and In Vivo Characterization of Vaccine Adjuvants.ILAR journal · 2018Article
- Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An array of lipidic compounds that constitute the cell wall of mycobacteria is recognized by host receptors. Examples include trehalose dimycolate (TDM), which is a major surface-exposed glycolipid of mycobacteria, that interacts with the macrophage inducible C-type lectin, Mincle, and exerts its highly potent adjuvant functions. Recent evidence has suggested that glycerol monomycolate (GroMM), another mycolate-containing lipid species produced by mycobacteria, can stimulate innate immune cells; however, its specific host receptors have yet to be identified. We here demonstrated that cell transfectants expressing human Mincle (hMincle) reacted to both TDM and GroMM, while those expressing mouse Mincle (mMincle) only reacted to TDM and failed to recognize GroMM. Studies using domain swap chimeras confirmed that the ectodomain of hMincle, but not that of mMincle, interacted with GroMM, and site-directed mutagenesis analyses revealed that short stretches of amino acid residues at positions 174-176 and 195-196 were involved in GroMM recognition. To further substantiate the differential recognition of GroMM by hMincle and mMincle, hMincle transgenic/mMincle knock-out mice (i.e. hMincle(+) mice) were established and compared with non-transgenic mice (i.e. mMincle(+) mice). We showed that macrophages derived from hMincle(+) mice were activated by GroMM and produced inflammatory cytokines, whereas those derived from mMincle(+) mice did not exhibit any reactivity to GroMM. Furthermore, local inflammatory responses were elicited in the GroMM-injected skin of hMincle(+), but not mMincle(+) mice. These results demonstrated that GroMM is a unique ligand for hMincle that is not recognized by mMincle.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.