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CD8αα and ‐αβ isotypes are equally recruited to the immunological synapse through their ability to bind to MHC class I
Author(s) -
Rybakin Vasily,
Clamme JeanPierre,
Ampudia Jeanette,
Yachi Pia P,
Gascoigne Nicholas R J
Publication year - 2011
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2011.209
Subject(s) - mhc class i , class (philosophy) , biology , mhc class ii , immunological synapse , cd8 , major histocompatibility complex , synapse , microbiology and biotechnology , virology , genetics , immunology , computational biology , neuroscience , immune system , t cell , computer science , t cell receptor , artificial intelligence
Bimolecular fluorescence complementation was used to engineer CD8 molecules so that CD8αα and CD8αβ dimers can be independently visualized on the surface of a T cell during antigen recognition. Using this approach, we show that CD8αα is recruited to the immunological synapse almost as well as CD8αβ, but because the kinase Lck associates preferentially with CD8αβ in lipid rafts, CD8αα is the weaker co‐receptor. During recognition of the strong CD8αα ligand H2‐TL, CD8αα is preferentially recruited. Thus, recruitment of the two CD8 species correlates with their relative binding to the available ligands, rather than with the co‐receptor functions of the CD8 species.