2 Works

Data from: Empty conformers of HLA-B preferentially bind CD8 and regulate CD8+ T cell function

Jie Geng, John D. Altman, Sujatha Krishnakumar & Malini Raghavan
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-B35:01, peptide-deficient (empty) heterodimers are thermostable and detectable on the cell surface. Additionally, peptide-deficient HLA-B35:01 tetramers preferentially bind CD8 and to a majority of blood-derived CD8+ T...

Data from: Variations in HLA-B cell surface expression, half-life and extracellular antigen receptivity

Brogan Yarzabek, Anita J. Zaitouna, Eli Olson, Gayathri N. Silva, Jie Geng, Aviva Geretz, Rasmi Thomas, Sujatha Krishnakumar, Daniel S. Ramon & Malini Raghavan
The highly polymorphic human leukocyte antigen (HLA) class I molecules present peptide antigens to CD8+ T cells, inducing immunity against infections and cancers. Quality control mediated by peptide loading complex (PLC) components is expected to ensure the cell surface expression of stable peptide-HLA class I complexes. This is exemplified by HLA-B*08:01 in primary human lymphocytes, with both expression level and half-life at the high end of the measured HLA-B expression and stability hierarchies. Conversely, low...

Registration Year

  • 2018
    2

Resource Types

  • Dataset
    2

Affiliations

  • University of Michigan-Ann Arbor
    2
  • Immucor (United States)
    2
  • Emory University School of Medicine
    1
  • Walter Reed Army Institute of Research
    1
  • Mayo Clinic
    1