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https://scholarbank.nus.edu.sg/handle/10635/13945
DC Field | Value | |
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dc.title | Comparative study of HLA-B27 peptide binding specificity by in vitro refolding assay | |
dc.contributor.author | QIU CHONGWEI | |
dc.date.accessioned | 2010-04-08T10:38:19Z | |
dc.date.available | 2010-04-08T10:38:19Z | |
dc.date.issued | 2004-05-09 | |
dc.identifier.citation | QIU CHONGWEI (2004-05-09). Comparative study of HLA-B27 peptide binding specificity by in vitro refolding assay. ScholarBank@NUS Repository. | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/13945 | |
dc.description.abstract | HLA-B27 is strongly associated with predisposition to ankylosing spondylitis and reactive arthritis, but the mechanism of pathogenesis remains a mystery. There are experimental evidences supporting the hypothesis of an a??arthritogenica?? peptide which induces an anti-self response. In this study, we used an in vitro refolding assay to reconstitute the HLA-B27/peptide complex to precisely define the effects of variability at the C-terminal anchor residue of a synthetic nonapeptide on its binding affinity to HLA-B27 subtypes. Out results showed that among the 20 variants of the nonapeptide, non-polar amino acid is clearly preferred at the C-terminal anchor. The disease associated subtypes B*2702, B*2704 and B*2705 bound C-terminal tyrosine strongly, while B*2706 and B*2709 which are negatively associated with disease displayed poor affinity for C-terminal tyrosine. Overall, the pattern of in vitro refolded HLA-B27/peptide complexes showed remarkable agreement with known data derived from mass spectrometry analysis of recovered naturally bound peptide ligands. | |
dc.language.iso | en | |
dc.subject | ankylosing spondylitis, HLA-B27, subtypes, polymorphism, peptide binding, peptide specificity | |
dc.type | Thesis | |
dc.contributor.department | MICROBIOLOGY | |
dc.contributor.supervisor | REN EE CHEE | |
dc.description.degree | Master's | |
dc.description.degreeconferred | MASTER OF SCIENCE | |
dc.identifier.isiut | NOT_IN_WOS | |
Appears in Collections: | Master's Theses (Open) |
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QiuCW.pdf | 8.3 MB | Adobe PDF | OPEN | None | View/Download |
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