HLA-G protein processing and transport to the cell surface |
| |
Authors: | P Moreau P Rousseau N Rouas-Freiss M Le Discorde J Dausset E D Carosella |
| |
Institution: | 1.CEA, Service de Recherche en Hémato-Immunologie, DSV/DRM, H?pital Saint-Louis, Institut Universitaire d'Hématologie, 1 avenue Claude Vellefaux, 75010 Paris (France), Fax +33(0)1 48 03 19 60, e-mail: moreau@dsvidf.cea.fr,FR;2.Fondation Jean Dausset, 27 rue Juliette-Dodu, 75010 Paris (France),FR |
| |
Abstract: | Data are presented on the intracellular trafficking of HLA-G protein, taking the unique features of this non-classical molecule
into consideration: the existence of seven isoforms resulting from alternative splicing (HLA-G1 to G7), and reduced tail length
compared with HLA class I antigens. Biochemical studies and analysis of viral strategies for escaping the host immune system
led to the demonstration that (i) both the membrane-bound (HLA-G1) and the soluble (HLA-G5) forms of the molecule require
peptide association for cell surface expression, using TAP-dependent or TAP-independent pathways; (ii) peptide loading onto
the HLA-G protein plays a critical role in controlling the quality of the molecule reaching the cell surface; (iii) surface
expression of truncated HLA-G molecules is possible, and (iv) HLA-G expression may be restricted to soluble HLA-G5. These
data reveal that HLA-G presents specific cell trafficking pathways and strongly support the contention that the primary function
of HLA-G is as of an inhibitor ligand for immune-competent cells.
Received 4 June 2002; accepted 2 July 2002
RID="*"
ID="*"Corresponding author. |
| |
Keywords: | , HLA-G isoform, intracellular traffic, function, |
本文献已被 PubMed SpringerLink 等数据库收录! |
|