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Published Erratum
. 2019 Apr 9;116(15):7592-7593.
doi: 10.1073/pnas.1904079116. Epub 2019 Apr 1.

Correction for Bandala-Sanchez et al., CD52 glycan binds the proinflammatory B box of HMGB1 to engage the Siglec-10 receptor and suppress human T cell function

No authors listed
Published Erratum

Correction for Bandala-Sanchez et al., CD52 glycan binds the proinflammatory B box of HMGB1 to engage the Siglec-10 receptor and suppress human T cell function

No authors listed. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 4.
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.
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