The abstract is read at the publisher; the summary is JClub's.
A conserved TRBV4-1 or TRBV7-9 TCR motif is found in more than half of sequenced CD1c–mycoketide tetramer+ αβ TCRs, enabling recognition of CD1c-presented phospholipid antigen.
- Why it matters: The way αβ T cells recognize mycobacterial lipids on CD1 family molecules is unclear, limiting understanding of how protective or disease-linked immune responses are shaped.
- What they did: CD1c tetramers loaded with phosphomycoketide (PM) or mannosyl-PM were used to isolate T cells from healthy donors and individuals from a TB-endemic region of South Africa, followed by high-throughput sequencing of >200 paired CD1c-mycoketide tetramer+ αβ TCRs and cryo-EM of a TRBV7-9+ TCR bound to CD1c–PM.
- The result: The TRBV7-9+ TCR docks on the A'-side of CD1c, contacting the phospholipid antigen and F'-portal residues, and mutant-based clone analyses suggest this docking mode represents the larger TRBV7-9+ population.
The findingWhy it mattersWhat they didThe result
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