{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,31]],"date-time":"2026-03-31T03:38:16Z","timestamp":1774928296605,"version":"3.50.1"},"reference-count":36,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2003,2,4]],"date-time":"2003-02-04T00:00:00Z","timestamp":1044316800000},"content-version":"vor","delay-in-days":3,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Arthritis &amp; Rheumatism"],"published-print":{"date-parts":[[2003,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>Objective<\/jats:title><jats:p>To assess the binding of outer surface protein A (OspA) and human lymphocyte function\u2013associated antigen 1 (hLFA\u20101) peptides to 5 major histocompatibility complex (MHC) molecules.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>Peptide binding to the MHC molecules was determined by in vitro binding assays, and binding was correlated with the frequencies of the 5 MHC molecules in patients with treatment\u2010resistant Lyme arthritis.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>The HLA\u2013DRB1*0401 molecule bound both OspA<jats:sub>163\u2013175<\/jats:sub> and hLFA\u20101\u03b1<jats:sub>L330\u2013342<\/jats:sub> well. Although the magnitude of the binding was less, the DRB1*0404 molecule also showed binding of both peptides. The DRB1*0101 molecule bound OspA<jats:sub>163\u2013175<\/jats:sub> well, but hLFA\u20101\u03b1<jats:sub>L330\u2013342<\/jats:sub> only weakly; the DRB1*0801 or *1101 molecule bound both peptides weakly, if at all. The magnitude of OspA<jats:sub>163\u2013175<\/jats:sub> binding correlated well with the frequencies of the DRB1 alleles in patients with treatment\u2010resistant arthritis, but the binding of hLFA\u20101\u03b1<jats:sub>L330\u2013342<\/jats:sub> showed only an association with the DRB*04 alleles.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion<\/jats:title><jats:p>These correlations support the hypothesis that OspA<jats:sub>163\u2013175<\/jats:sub> is the critical epitope in triggering antibiotic treatment\u2013resistant Lyme arthritis. However, the inability of the DRB*0101 molecule to bind hLFA\u20101\u03b1<jats:sub>L330\u2013342<\/jats:sub> suggests that this peptide may not be a relevant autoantigen, at least in DRB1*0101\u2010positive patients.<\/jats:p><\/jats:sec>","DOI":"10.1002\/art.10772","type":"journal-article","created":{"date-parts":[[2003,2,7]],"date-time":"2003-02-07T07:09:02Z","timestamp":1044601742000},"page":"534-540","source":"Crossref","is-referenced-by-count":84,"title":["Binding of outer surface protein A and human lymphocyte function\u2013associated antigen 1 peptides to HLA\u2013DR molecules associated with antibiotic treatment\u2013resistant Lyme arthritis"],"prefix":"10.1002","volume":"48","author":[{"given":"Allen C.","family":"Steere","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ben","family":"Falk","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elise 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