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

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 expression on lymphocytes is measured for
three HLA-B allotypes that bind peptides with proline at position 2, which
are disfavored by the transporter associated with antigen processing.
Surprisingly, these lymphocyte-specific expression and stability
differences become reversed or altered in monocytes, which display larger
intracellular pools of HLA class I than lymphocytes. Together, the
findings indicate that allele and cell-dependent variations in antigen
acquisition pathways influence HLA-B surface expression levels, half-lives
and receptivity to exogenous antigens.