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Stable expression of MHC class I heavy chain/HLA‐DO complexes at the plasma membrane
Author(s) -
van Lith Marcel,
van Ham Marieke,
Neefjes Jacques
Publication year - 2003
Publication title -
european journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.272
H-Index - 201
eISSN - 1521-4141
pISSN - 0014-2980
DOI - 10.1002/eji.200323472
Subject(s) - major histocompatibility complex , endoplasmic reticulum , mhc class i , biology , human leukocyte antigen , transporter associated with antigen processing , beta 2 microglobulin , cd74 , microbiology and biotechnology , antigen processing , antigen presentation , immune system , heavy chain , transfection , antigen , gene , immunology , genetics , t cell
Abstract Major histocompatibility complex (MHC) class I and II molecules present antigenic fragments to the immune system. MHC‐like chaperones, like HLA‐DM, HLA‐DO and tapasin support peptide loading. HLA class I heavy chains require association with β2‐microglobulin and peptide for endoplasmic reticulum (ER) exit. Likewise, HLA‐DO is only able to leave the ER by association to DM. Here we show that HLA‐DO and free MHC class I heavy chains associate into a stable complex early during biosynthesis and are expressed at the plasma membrane as a complex. These DO/heavy chain complexes are found on DO‐transfected cells and on low amounts on human B cells.