{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T11:09:30Z","timestamp":1790766570317,"version":"4.1.0"},"reference-count":42,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2007,6,28]],"date-time":"2007-06-28T00:00:00Z","timestamp":1182988800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Arthritis &amp; Rheumatism"],"published-print":{"date-parts":[[2007,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>Objective<\/jats:title><jats:p>To examine whether and to what extent the intracellular trafficking features of HLA\u2013B*2705, which is associated with the development of spondylarthritis (SpA), differ from those of HLA\u2013B*2709 and HLA\u2013B*0702, which are not associated with SpA.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>HeLa cells were transfected with complementary DNA encoding for HLA\u2013B proteins fused to <jats:italic>Renilla<\/jats:italic> luciferase or yellow fluorescent protein. The subcellular distribution of properly folded and unfolded\/misfolded HLA\u2013B proteins was examined by flow cytometry and confocal microscopy of cells labeled with ME1 and HC\u201010 antibodies, respectively. HLA\u2013B\/HLA\u2013B interactions were monitored in endoplasmic reticulum (ER)\u2013 and plasma membrane\u2013enriched subcellular fractions, by bioluminescence resonance energy transfer (BRET).<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>All 3 HLA\u2013B alleles displayed a similar distribution pattern (properly folded heavy chain at the cell surface, unfolded\/misfolded proteins only in the cytoplasm). By means of BRET, we provided evidence that both HLA\u2013B*2705 and HLA\u2013B*2709 formed more oligomers in the ER and the plasma membrane than did HLA\u2013B*0702. The propensity of HLA\u2013B*2705 to form oligomers in the ER was partly attributable to residue Cys<jats:sup>67<\/jats:sup> of the molecule. For all 3 alleles, increased expression of HLA\u2013B proteins was associated with intracytoplasmic accumulation of unfolded\/misfolded proteins and intracellular vesicles, probably corresponding to expanded ER\u2013Golgi intermediate compartments, in which these proteins accumulated together with the stress sensor BiP.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion<\/jats:title><jats:p>Our results suggest that the difference in disease susceptibility conferred by HLA\u2013B*2705 and HLA\u2013B*2709 cannot be explained by their different propensity to form dimers or misfolded proteins, thus presumably implicating other, still unknown factors.<\/jats:p><\/jats:sec>","DOI":"10.1002\/art.22725","type":"journal-article","created":{"date-parts":[[2007,6,28]],"date-time":"2007-06-28T17:47:03Z","timestamp":1183052823000},"page":"2232-2243","source":"Crossref","is-referenced-by-count":16,"title":["Two HLA\u2013B27 alleles differently associated with spondylarthritis, B*2709 and B*2705, 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