Study uncovers the complexities of how CD1 molecules present a vast array of lipids to T-cells, revealing a unique, size-based antigen-display system. The findings could provide crucial insights into the intricacies of immune response and antigen presentation.
By Tarun Sai LomteSep 21 2023Reviewed by Benedette Cuffari, M.Sc. In a recent study published in the journal Cell, researchers identify lipidomes as four cluster of differentiation 1 antigen-presenting molecules and, as a result, reveal a map of self-lipid display.
These isoforms fold and form narrow portals that lead to internal hydrophobic clefts binding the alkyl chains of lipids. High throughput detection of lipids bound to CD1 isoforms may distinguish whether the isoforms capture the same or different lipids, whether they are specific lipid receptors, or instead broadly survey the cellular lipidome.
Between 404-580, unique CD1 ligands were captured per isoform, which resulted in 1,841 and 2,256 unique CD1-lipid pairs in the two datasets. Chemical identification of molecules bound to multiple isoforms was required to determine the molecular determinants of isoform-specific ligand capture. Long-chain, intermediate-chain, and shortest PCs skewed to CD1d, CD1a, and CD1b, respectively. However, CD1c had equivalent capture of PCs of all lengths found in cells.
The number of CH2 units inside CD1 clefts. CD1a bound an average of C16.7 for single-tailed ligands or C38.3 for two-tailed ligands. The ligand size of other isoforms was significantly variable.
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