Conformation of human leucocyte antigen-C molecules at the surface of human trophoblast cells.

Publisher: Blackwell Scientific Publications Country of Publication: England NLM ID: 0374672 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1365-2567 (Electronic) Linking ISSN: 00192805 NLM ISO Abbreviation: Immunology Subsets: MEDLINE

Original Publication: Oxford : Blackwell Scientific Publications

HLA-C Antigens/*chemistry ; Trophoblasts/*immunology; Female ; Flow Cytometry/methods ; HLA Antigens/chemistry ; HLA Antigens/immunology ; HLA-C Antigens/immunology ; HLA-G Antigens ; Histocompatibility Antigens Class I/chemistry ; Histocompatibility Antigens Class I/immunology ; Humans ; Immunoprecipitation ; Pregnancy ; Protein Conformation ; Protein Denaturation ; Tumor Cells, Cultured ; beta 2-Microglobulin/metabolism

Human leucocyte antigen (HLA)-C is expressed at lower levels than other classical HLA-I molecules on somatic cells. Surface HLA-C proteins can occur as conventionally beta(2)-microglobulin (beta2m)-associated complexes or as open conformers dissociated from peptide and/or beta(2)m. We investigated the conformation of HLA-C molecules on normal human trophoblast cells, which invade the maternal decidua during placentation. A panel of monoclonal antibodies to different conformations of HLA-I molecules was used in flow cytometry and surface immunoprecipitation experiments. On the surface of trophoblast cells only beta(2)m-associated complexes of HLA-C molecules were detected. In contrast, both open conformers and beta(2)m-associated HLA-C could be detected on other cells from the decidua, HLA-C-transfectants and cell lines. The levels of HLA-C expressed on primary trophoblast cells could be detected by antibodies specific to non-beta(2)m-associated conformations because binding was seen after acid-induced denaturation of surface proteins. In contrast to HLA-G molecules on trophoblasts, we found no evidence for the presence of disulphide-linked multimers of HLA-C complexes. These results show that most HLA-C molecules present at the trophoblast cell surface are in the conventional beta(2)m-associated conformation. These findings have implications regarding the stability of trophoblast HLA-C molecules and how they interact with receptors on decidual leucocytes during placentation.

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United Kingdom Wellcome Trust

0 (HLA Antigens)
0 (HLA-C Antigens)
0 (HLA-G Antigens)
0 (Histocompatibility Antigens Class I)
0 (beta 2-Microglobulin)

Date Created: 20080122 Date Completed: 20080811 Latest Revision: 20211020

20221213

PMC2440826

10.1111/j.1365-2567.2007.02789.x

18205788