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Increased Conformational Flexibility of HLA-B*27 Subtypes Associated With Ankylosing Spondylitis.

Loll B, Fabian H, Huser H, Hee CS, Ziegler A, Uchanska-Ziegler B, Ziegler A
Arthritis Rheumatol 68 1172-82 (2016)
Cited: 20 times
EuropePMC logo PMID: 26748477

Abstract

Objective

Dissimilarities in antigen processing and presentation are known to contribute to the differential association of HLA-B*27 subtypes with the inflammatory rheumatic disease ankylosing spondylitis (AS). In support of this notion, previous x-ray crystallographic data showed that peptides can be displayed by almost identical HLA-B*27 molecules in a subtype-dependent manner, allowing cytotoxic T lymphocytes to distinguish between these subtypes. For example, a human self-peptide derived from vasoactive intestinal peptide receptor type 1 (pVIPR; sequence RRKWRRWHL) is displayed in a single conformation by B*27:09 (which is not associated with AS), while B*27:05 (which is associated with AS) presents the peptide in a dual binding mode. In addition, differences in conformational flexibility between these subtypes might affect their stability or antigen presentation capability. This study was undertaken to investigate B*27:04 and B*27:06, another pair of minimally distinct HLA-B*27 subtypes, to assess whether dual peptide conformations or structural dynamics play a role in the initiation of AS.

Methods

Using x-ray crystallography, we determined the structures of the pVIPR-B*27:04 and pVIPR-B*27:06 complexes and used isotope-edited infrared (IR) spectroscopy to probe the dynamics of these HLA-B*27 subtypes.

Results

As opposed to B*27:05 and B*27:09, B*27:04 (which is associated with AS) displays pVIPR conventionally and B*27:06 (which is not associated with AS) presents the peptide in a dual conformation. Comparison of the 4 HLA-B*27 subtypes using IR spectroscopy revealed that B*27:04 and B*27:05 possess elevated molecular dynamics compared to the nonassociated subtypes B*27:06 and B*27:09.

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Reviews citing this publication (7)

  1. Ankylosing Spondylitis and Axial Spondyloarthritis. Taurog JD, Chhabra A, Colbert RA. N Engl J Med 374 2563-2574 (2016)
  2. Causes and consequences of endoplasmic reticulum stress in rheumatic disease. Navid F, Colbert RA. Nat Rev Rheumatol 13 25-40 (2017)
  3. The Early Phases of Ankylosing Spondylitis: Emerging Insights From Clinical and Basic Science. Watad A, Bridgewood C, Russell T, Marzo-Ortega H, Cuthbert R, McGonagle D. Front Immunol 9 2668 (2018)
  4. The interplay between HLA-B27 and ERAP1/ERAP2 aminopeptidases: from anti-viral protection to spondyloarthritis. Vitulano C, Tedeschi V, Paladini F, Sorrentino R, Fiorillo MT. Clin Exp Immunol 190 281-290 (2017)
  5. Three-Dimensional Portable Document Format (3D PDF) in Clinical Communication and Biomedical Sciences: Systematic Review of Applications, Tools, and Protocols. Newe A, Becker L. JMIR Med Inform 6 e10295 (2018)
  6. Uncovering the Underworld of Axial Spondyloarthritis. Del Vescovo S, Venerito V, Iannone C, Lopalco G. Int J Mol Sci 24 6463 (2023)
  7. HLA-B*27 and Ankylosing Spondylitis: 50 Years of Insights and Discoveries. Khan MA. Curr Rheumatol Rep 25 327-340 (2023)

Articles citing this publication (11)

  1. Polymorphisms in the F Pocket of HLA-B27 Subtypes Strongly Affect Assembly, Chaperone Interactions, and Heavy-Chain Misfolding. Guiliano DB, North H, Panayoitou E, Campbell EC, McHugh K, Cooke FG, Silvestre M, Bowness P, Powis SJ, Antoniou AN. Arthritis Rheumatol 69 610-621 (2017)
  2. The Role of Autophagy in the Degradation of Misfolded HLA-B27 Heavy Chains. Navid F, Layh-Schmitt G, Sikora KA, Cougnoux A, Colbert RA. Arthritis Rheumatol 70 746-755 (2018)
  3. The molecular basis of how buried human leukocyte antigen polymorphism modulates natural killer cell function. Saunders PM, MacLachlan BJ, Pymm P, Illing PT, Deng Y, Wong SC, Oates CVL, Purcell AW, Rossjohn J, Vivian JP, Brooks AG. Proc Natl Acad Sci U S A 117 11636-11647 (2020)
  4. Conformational Plasticity of HLA-B27 Molecules Correlates Inversely With Efficiency of Negative T Cell Selection. Loll B, Rückert C, Uchanska-Ziegler B, Ziegler A. Front Immunol 11 179 (2020)
  5. Preferential HLA-B27 Allorecognition Displayed by Multiple Cross-Reactive Antiviral CD8+ T Cell Receptors. Rowntree LC, van den Heuvel H, Sun J, D'Orsogna LJ, Nguyen THO, Claas FHJ, Rossjohn J, Kotsimbos TC, Purcell AW, Mifsud NA. Front Immunol 11 248 (2020)
  6. Human Leukocyte Antigen C*12:02:02 and Killer Immunoglobulin-Like Receptor 2DL5 are Distinctly Associated with Ankylosing Spondylitis in the Taiwanese. Wang CM, Wang SH, Jan Wu YJ, Lin JC, Wu J, Chen JY. Int J Mol Sci 18 E1775 (2017)
  7. Metal-triggered conformational reorientation of a self-peptide bound to a disease-associated HLA-B*27 subtype. Driller R, Ballaschk M, Schmieder P, Uchanska-Ziegler B, Ziegler A, Loll B. J Biol Chem 294 13269-13279 (2019)
  8. Increased proportions of inflammatory T cells and their correlations with cytokines and clinical parameters in patients with ankylosing spondylitis from northern Sweden. Lejon K, Hellman U, Do L, Kumar A, Forsblad-d'Elia H. Scand J Immunol 96 e13190 (2022)
  9. HLA-C*12:02 is strongly associated with Xuesaitong-induced cutaneous adverse drug reactions. Yan S, Xiong H, Shao F, Zhang W, Yang F, Qi Z, Chen S, He L, Jiang M, Su Y, Zhu H, Qin S, Zhu Q, Luo X, Xing Q. Pharmacogenomics J 19 277-285 (2019)
  10. Intrinsic Folding Properties of the HLA-B27 Heavy Chain Revealed by Single Chain Trimer Versions of Peptide-Loaded Class I Major Histocompatibility Complex Molecules. Lenart I, Truong LH, Nguyen DD, Rasiukienė O, Tsao E, Armstrong J, Kumar P, McHugh K, Pereira BI, Maan BS, Garstka MA, Bowness P, Blake N, Powis SJ, Gould K, Nesbeth D, Antoniou AN. Front Immunol 13 902135 (2022)
  11. Case Reports Management of pregnancy complicated by ankylosing spondylitis: A case report and literature review. Midorikawa A, Wang L, Kuwata T, Taniguchi Y, Horiuchi I, Matsushita C, Chikazawa K, Takagi K. Clin Case Rep 7 766-769 (2019)


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