IMMUNOLOGY AND INFLAMMATION Correction for “CD52 glycan binds the proinflammatory B box of HMGB1 to engage the Siglec-10 receptor and suppress human T cell function,” by Esther Bandala-Sanchez, Naiara G. Bediaga, Ethan D. Goddard-Borger, Katrina Ngui, Gaetano Naselli, Natalie L. Stone, Alana M. Neale, Lesley A. Pearce, Ahmad Wardak, Peter Czabotar, Thomas Haselhorst, Andrea Maggioni, Lauren A. Hartley-Tassell, Timothy E. Adams, and Leonard C. Harrison, which was first published July 11, 2018; 10.1073/pnas.1722056115 (Proc Natl Acad Sci USA 115:7783–7788).
The authors note that Fig. 4 appeared incorrectly. The corrected figure and its legend appear below.
Fig. 4.
CD52-Fc glycan sialic acid is required for binding to HMGB1 and Siglec-10. (A) Binding of CD52-Fc, pretreated with Clostridium perfringens type V neuraminidase or with vehicle alone, to plate-bound proteins or combinations of proteins as indicated. (B) Binding of untreated CD52-Fc to lectins (MAA I, MAA II, and SNA) immobilized on a microtiter plate, showing that CD52-Fc binds MAA I, a lectin that recognizes sialic acid in α-2,3 linkage with galactose. (C) Resialylation of neuraminidase-treated CD52-Fc with either α-2,3 (CstII) or α-2,6 (PdST6Ga1I) sialyltransferases, confirmed by binding to MAA I lectin (α-2,3 linkage) or SNA lectin (α-2,6 linkage). (D) ELISpot assay demonstrating functional activity of CD52-Fc reconstituted with sialic acid in α-2,3 linkage with galactose. Data are mean ± SEM of three independent experiments.