Open AccessThe T cell antigen receptor expressed by Vα14iNKT cells has a unique mode of glycosphingolipid antigen recognition
Author(s) -
Stéphane Sidobre,
Kirsten J. L. Hammond,
Lise Bénazet-Sidobre,
Sergei D. Maltsev,
Stewart K. Richardson,
Rachel M. Ndonye,
Amy R. Howell,
Teruyuki Sakai,
Gurdyal S. Besra,
Steven A. Porcelli,
Mitchell Kronenberg
Publication year - 2004
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0404632101
Subject(s) - cd1d , natural killer t cell , glycosphingolipid , t cell receptor , glycolipid , antigen , biology , ceramide , microbiology and biotechnology , t cell , cd1 , population , receptor , immunology , biochemistry , immune system , medicine , cd8 , apoptosis , environmental health
Natural killer (NK) T cells with an invariant Valpha14 rearrangement (Valpha14i) are the largest population of lipid antigen-specific T lymphocytes identified in animals. They react to the glycolipid alpha-galactosyl ceramide (alpha-GalCer) presented by CD1d, and they may have important regulatory functions. It was previously shown that the Valpha14i T cell antigen receptor (TCR) has a high affinity for the alpha-GalCer/CD1d complex, driven by a long half-life (t(1/2)). Although this result could have reflected the unique attributes of alpha-GalCer, using several related glycolipid compounds, we show here that the threshold for full activation of Valpha14i NKT cells by these glycosphingolipids requires a relatively high-affinity TCR interaction with a long t(1/2). Furthermore, our data are consistent with the view that the mechanism of recognition of these compounds presented by CD1d to the Valpha14i NKT cell TCR is likely to fit a lock-and-key model. Overall, these findings emphasize the distinct properties of glycosphingolipid antigen recognition by Valpha14i NKT cells.