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Showing 1–13 of 13 results
Advanced filters: Author: Tan-Yun Cheng Clear advanced filters
  • Despite extensive structural studies elucidating how antigens are anchored to antigen-presenting molecules and presented to T cells, little is known about the display mechanism of the lipid-antigen-presenting molecule CD1c. Here, by combining structural immunology, lipidomics, and biophysical analysis, the authors reveal that the CD1c binding cleft accommodates two different lipids, one of them with a bulky headgroup positioned sideways for display to T cells, rather than upwards, different from the conventional upright antigen-presentation mode

    • Thinh-Phat Cao
    • Guan-Ru Liao
    • Jamie Rossjohn
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-14
  • Buter et al. elucidated the biological function of the terpene nucleoside 1-TbAd, which is made abundantly by virulent but not avirulent Mycobacterium tuberculosis strains, and demonstrate that 1-TbAd regulates the pH and function of host macrophage endolysosomes.

    • Jeffrey Buter
    • Tan-Yun Cheng
    • D. Branch Moody
    Research
    Nature Chemical Biology
    Volume: 15, P: 889-899
  • Fibroblasts play critical roles in tissue homeostasis, but in pathologic states they can drive fibrosis, inflammation, and tissue destruction. Here, Faust et al. find that healthy human synovial fibroblasts under the influence of adjacent adipocytes have altered lipid metabolism driven by cortisol signaling. Both adipocytes and these characteristics are lost in inflammatory arthritis.

    • Heather J. Faust
    • Tan-Yun Cheng
    • Michael B. Brenner
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-20
  • De Jong and colleagues identify staphylococcal phosphatidylglycerol lipids as antigens for human CD1a-restricted T cells, which promote type 2 immune responses and may contribute to atopic dermatitis.

    • Gwennaëlle C. Monnot
    • Marcin Wegrecki
    • Annemieke de Jong
    Research
    Nature Immunology
    Volume: 24, P: 110-122
  • CD1 proteins present lipid antigens to T cells via the T cell receptor. Here the authors describe T cell reactivity to human membrane lipid moieties and provide structural data to define a molecular mechanism of promiscuous recognition of self-derived phospholipids.

    • Adam Shahine
    • Peter Reinink
    • Ildiko Van Rhijn
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12
  • Toll-like receptor 2 is activated by triacylated lipoproteins, but structural and functional studies now show that Mycobacterium tuberculosis lipoprotein LprG is a TLR2 agonist even when it is non-acylated. LprG contains a hydrophobic pocket to bind triacylated glycolipids and delivers them to TLR2, perhaps via CD14. In addition, LprG may serve as a glycolipid chaperone in cell wall assembly by Mycobacterium tuberculosis.

    • Michael G Drage
    • Han-Chun Tsai
    • Clifford V Harding
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 1088-1095
  • Germline-encoded mycolyl lipid-reactive (GEM) T cells recognize CD1b proteins presenting mycobacterial mycolates via their T-cell receptors (TCRs). Here, the authors present the structure of this interaction and provide a molecular basis for the co-recognition of CD1b and a mycobacterial glycolipid.

    • Stephanie Gras
    • Ildiko Van Rhijn
    • Jamie Rossjohn
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-12
  • CD1 molecules present diverse lipid ligands to TCRs expressed by NKT cells. Rossjohn, Moody and colleagues show a unique form of autoreactivity with human CD1c molecules, whereby TCRs recognize a closed conformation of CD1c molecules, which are loaded with a diverse array of ‘headless’ glycolipids.

    • Kwok S. Wun
    • Josephine F. Reijneveld
    • Jamie Rossjohn
    Research
    Nature Immunology
    Volume: 19, P: 397-406
  • CD1a presents a broad repertoire of lipid-based antigens. Rossjohn and colleagues show that the TCR docks over CD1a in a manner that precludes contact with permissive antigens, while nonpermissive antigens disrupt the TCR-CD1a contact.

    • Richard W Birkinshaw
    • Daniel G Pellicci
    • Jamie Rossjohn
    Research
    Nature Immunology
    Volume: 16, P: 258-266