HLA-B27 heavy chains distinguished by a micropolymorphism exhibit differential flexibility

Arthritis and Rheumatism
Heinz FabianBarbara Uchanska-Ziegler

Abstract

Although the products of the HLA subtypes B*2705 and B*2709 differ only in residue 116 (Asp versus His) within their peptide-binding grooves, they are differentially associated with inflammatory rheumatic diseases such as ankylosing spondylitis (AS): B*2705 occurs in AS patients, whereas B*2709 is only rarely encountered. The reasons for this distinct association are still unclear but could include subtype-specific conformational and dynamic properties of these antigens. The present study was undertaken to investigate structural and dynamic differences between B*2705 and B*2709 and their possible relationship to subtype-specific disease association. The membrane-distal segments of the B*2705 and B*2709 heavy chains were expressed in vitro and reconstituted together with beta(2)-microglobulin and a peptide. HLA-B27 complexes loaded with 2 self peptides (TIS [RRLPIFSRL] and pVIPR [RRKWRRWHL]) and a sequence-related viral peptide (pLMP2 [RRRWRRLTV]) were studied by isotope-edited infrared spectroscopy to detect differences in their structure and flexibility at physiologic temperature. Our analyses revealed the existence of subtype-specific conformational differences between the 2 HLA-B27 heavy chains at physiologic temperature, wh...Continue Reading

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Aug 7, 2013·Molecular Immunology·Rosa SorrentinoMaria Teresa Fiorillo
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Dec 23, 2020·International Journal of Molecular Sciences·Valentina TedeschiMaria Teresa Fiorillo
Jun 22, 2021·Current Opinion in Immunology·Hau V Truong, Nikolaos G Sgourakis

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