Abstract：
:CD1 proteins are expressed on dendritic cells, where they display lipid antigens to T-cell receptors (TCRs). Here we describe T-cell autoreactivity towards ubiquitous human membrane phospholipids presented by CD1b. These T-cells discriminate between two major types of lipids, sphingolipids and phospholipids, but were broadly cross-reactive towards diverse phospholipids including phosphatidylcholine, phosphatidylinositol and phosphatidylethanolamine. The crystal structure of a representative TCR bound to CD1b-phosphatidylcholine provides a molecular mechanism for this promiscuous recognition. We observe a lateral escape channel in the TCR, which shunted phospholipid head groups sideways along the CD1b-TCR interface, without contacting the TCR. Instead the TCR recognition site involved the neck region phosphate that is common to all major self-phospholipids but absent in sphingolipids. Whereas prior studies have focused on foreign lipids or rare self-lipids, we define a new molecular mechanism of promiscuous recognition of common self-phospholipids including those that are known targets in human autoimmune disease.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Shahine A,Reinink P,Reijneveld JF,Gras S,Holzheimer M,Cheng TY,Minnaard AJ,Altman JD,Lenz S,Prandi J,Kubler-Kielb J,Moody DB,Rossjohn J,Van Rhijn Idoi
10.1038/s41467-018-07898-0subject
Has Abstractpub_date
2019-01-04 00:00:00pages
56issue
1issn
2041-1723pii
10.1038/s41467-018-07898-0journal_volume
10pub_type
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