Authors
Thinh-Phat Cao, Caroline Soliman, Samuel J Redmond, Tori Tappen, Jade Kollmorgen, Qiji Geng, D Branch Moody, Thomas J Scriba, Adam P Uldrich, Adriaan J Minnaard, Chetan Seshadri, Hariprasad Venugopal, Adam Shahine, Jamie Rossjohn, Dale I Godfrey, Nicholas A Gherardin
Published in
The Journal of experimental medicine. Volume 223. Issue 12. Dec 07, 2026. Epub Nov 13, 2026.
Abstract
The mechanism by which αβ T cell receptors (TCRs) recognize mycobacterial lipids presented by CD1 family members is not well understood. We used CD1c tetramers loaded with the mycobacterial phosphomycoketide (PM) or mannosyl-PM to isolate T cells from healthy blood donors and individuals from a tuberculosis (TB)-endemic region of South Africa, with higher frequencies observed in individuals from the TB-endemic region. High-throughput analysis of >200 paired CD1c-mycoketide tetramer+ αβTCRs identified a conserved TCR motif, encoded by TRBV4-1 or TRBV7-9 variable region genes in greater than half of TCRs sequenced. A cryo-EM structure of a TRBV7-9+ TCR in complex with CD1c-PM demonstrated that the TCR bound to the A'-side of CD1c, directly contacting the phospholipid antigen and F'-portal residues. Analysis of multiple T cell clones interacting with CD1c mutants suggested that this TCR docking mode is representative of the larger TRBV7-9+ T cell population. Collectively, this study provides insight into mycobacterial lipid antigen recognition by αβ T cells restricted to CD1c.
PMID:
43024229
Bibliographic data and abstract were imported from PubMed on 14 Nov 2026.
Read full publication at:
Please sign in
to see all details.
Advertisement
Stats
- Recommendations n/a n/a positive of 0 vote(s)
- Views 2
- Comments 0