Empty conformers of HLA-B preferentially bind CD8 and regulate CD8⁺ T cell function.

ABSTRACT: When complexed with antigenic peptides, human leukocyte antigen (HLA) class I (HLA-I) molecules initiate CD8⁺ T cell responses via interaction with the T cell receptor (TCR) and co-receptor CD8. Peptides are generally critical for the stable cell surface expression of HLA-I molecules. However, for HLA-I alleles such as HLA-B*35:01, peptide-deficient (empty) heterodimers are thermostable and detectable on the cell surface. Additionally, peptide-deficient HLA-B*35:01 tetramers preferentially bind CD8 and to a majority of blood-derived CD8⁺ T cells via a CD8-dependent binding mode. Further functional studies reveal that peptide-deficient conformers of HLA-B*35:01 do not directly activate CD8⁺ T cells, but accumulate at the immunological synapse in antigen-indu

SUBMITTER: Geng J 

PROVIDER: S-EPMC5990358 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature