Impaired spontaneous endocytosis of HLA-G

Daniel M. Davis, Hugh T. Reyburn, Laszlo Pazmany, Isaac Chiu, Ofer Mandelboim, Jack L. Strominger*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

49 Scopus citations


HLA-G is a class Ib (non-classical) major histocompatibility complex (MHC) protein expressed at the maternal-fetal interface that inhibits natural killer (NK) cell-mediated lysis in an allotype independent manner. Here we report that the spontaneous endocytosis of HLA-G is severely reduced because of its short cytoplasmic tail. Class I (classical) MHC proteins on the surface of B cell transfectants detected by primary and secondary antibodies underwent endocytosis at a moderate rate, whereas HLA-G, chimeric proteins consisting of the extracellular domains of HLA-C with the C-terminal sequence of HLA-G, or glycophosphatidylinositol-tailed HLA-C proteins, were not efficiently internalized. In addition, a mutant of β2-microglobulin (Ser88Cys) that could be specifically labeled with Texas red (or other fluorescent probes) and exchanged into class I or class Ib MHC proteins was employed to study spontaneous internalization of MHC proteins by a non-perturbative method independent of an antibody ligand. These data are discussed in terms of both the role of HLA-G expressed on the fetal trophoblast and the function of the cytoplasmic tail in class I MHC proteins.

Original languageAmerican English
Pages (from-to)2714-2719
Number of pages6
JournalEuropean Journal of Immunology
Issue number10
StatePublished - Oct 1997
Externally publishedYes


  • Antigen presentation
  • Antigen processing
  • Cell trafficking
  • Fluorescence microscopy
  • Major histocompatibility complex


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