Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/11321
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dc.contributor.authorEwing, Cen
dc.contributor.authorEbringer, Ren
dc.contributor.authorTribbick, Gen
dc.contributor.authorGeysen, H Men
dc.date.accessioned2015-05-16T00:54:38Z
dc.date.available2015-05-16T00:54:38Z
dc.date.issued1990-05-01en
dc.identifier.citationThe Journal of Experimental Medicine; 171(5): 1635-47en
dc.identifier.govdoc2185331en
dc.identifier.otherPUBMEDen
dc.identifier.urihttps://ahro.austin.org.au/austinjspui/handle/1/11321en
dc.description.abstract74 overlapping peptides of varying lengths from Klebsiella pneumoniae nitrogenase reductase (residues 181-199) and from the HLA B27.1 molecule (residues 65-85) were synthesized and tested by ELISA against sera from HLA B27+ ankylosing spondylitis (AS) patients, and sera from HLA B27+ and HLA B27- healthy first-degree relatives. Antibody activity in AS sera to Klebsiella peptides of four to eight amino acids was maximal with the peptide NSRQTDR. Activity to HLA B27 peptides was maximal with the peptide KAKAQTDR (named epitope I). These peptides overlap with, but are proximal to the NH2 terminus from QTDRED, which is homologous in HLA B27.1 and K. pneumoniae nitrogenase reductase. A second weaker reactive site was noted in the HLA B27.1 peptides, proximal to the COOH terminus from the homologous sequence, namely peptide REDLRTLL (named epitope II). Little activity was seen against peptides that included the entire homologous sequence. Sera from 50 AS patients showed higher total Ig activity against peptides KAKAQTDR (p less than 0.001) and NSRQTDR (p less than 0.02) than did sera from 22 B27+ and 22 B27- healthy controls. These data indicate that AS patient sera contain antibodies that bind to K. pneumoniae nitrogenase peptides and HLA B27.1 peptides, and that there are at least two epitopes on HLA B27.1 in the alpha 1 domain, at the MHC groove region, that are autoantigenic in AS patients. Epitope I may be a site for crossreactivity between HLA B27 and Klebsiella.en
dc.language.isoenen
dc.subject.otherAmino Acid Sequenceen
dc.subject.otherAntibodies, Bacterial.immunologyen
dc.subject.otherAutoantibodies.immunologyen
dc.subject.otherEnzyme-Linked Immunosorbent Assayen
dc.subject.otherHLA-B27 Antigen.immunologyen
dc.subject.otherHumansen
dc.subject.otherKlebsiella pneumoniae.enzymology.immunologyen
dc.subject.otherMolecular Sequence Dataen
dc.subject.otherNitrogenase.immunologyen
dc.subject.otherOxidoreductasesen
dc.subject.otherReference Valuesen
dc.subject.otherSequence Homology, Nucleic Aciden
dc.subject.otherSpondylitis, Ankylosing.blood.immunologyen
dc.titleAntibody activity in ankylosing spondylitis sera to two sites on HLA B27.1 at the MHC groove region (within sequence 65-85), and to a Klebsiella pneumoniae nitrogenase reductase peptide (within sequence 181-199).en
dc.typeJournal Articleen
dc.identifier.journaltitleThe Journal of experimental medicineen
dc.identifier.affiliationDepartment of Medicine, University of Melbourne, Austin Hospital, Heidelberg, Victoria.en
dc.description.pages1635-47en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/2185331en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
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