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Ankylosing spondylitis (AS) is highly associated with the expression of human leukocyte antigen-B27 (HLA-B ∗ 27). HLA-B ∗ 27 heavy chain (B27-HC) has an intrinsic propensity to fold slowly, leading to the accumulation of the misfolded B27-HC in the endoplasmic reticulum (ER) and formation of the HLA-B ∗ 27 HC homodimer, (B27-HC) 2 , by a disulfide linkage at Cys-67. (B27-HC) 2  displayed on the cell surface can act as a ligand of the killer-cell Ig-like receptor (KIR3DL2). (B27-HC) 2  binds to KIR3DL2 of NK and Th17 cells and activates both cells, resulting in the activation of the IL-23/IL-17 axis to launch the inflammatory reaction in AS patients. However, activation of the IL-23/IL-17 axis originally derived from the HLA-B ∗ 27 misfolding in the ER needs to be characterized. In this study, we delivered two HLA-B ∗ 27-binding peptides, KRGILTLKY and SRYWAIRTR, into the ER by using a tat-derived peptide (GRKKRRQRRR)-His 6 -ubiquitin (THU) vehicle. Both peptides are derived from the human actin and nucleoprotein of influenza virus, respectively. Our results demonstrated that targeted delivery of both HLA-B ∗ 27-binding peptides into the ER can promote the HLA-B ∗ 27 folding, decrease the levels of (B27-HC) 2 , and suppress the activation of the IL-23/IL-17 axis in response to lipopolysaccharide. Our findings can provide a new therapeutic strategy in AS.

mediators of inflammation

Targeted Delivery of the HLA-B<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="M1"><mml:msup><mml:mrow /><mml:mrow><mml:mo>∗</mml:mo></mml:mrow></mml:msup></mml:math>27-Binding Peptide into the Endoplasmic Reticulum Suppresses the IL-23/IL-17 Axis of Immune Cells in Spondylarthritis

Targeted Delivery of the HLA-B∗27-Binding Peptide into the Endoplasmic Reticulum Suppresses the IL-23/IL-17 Axis of Immune Cells in Spondylarthritis