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• W2102321925 endingPage "3003" @default.
• W2102321925 startingPage "2994" @default.
• W2102321925 abstract "CD22 (Siglec-2) is a key regulator of B cell signaling whose function is modulated by interaction with extracellular glycan ligands mediated through its N-terminal Ig domain. Its preferred ligand is the sequence Sia alpha2-6Gal that is abundantly expressed on N-linked glycans of B cell glycoproteins, and by binding to CD22 in cis causes CD22 to appear masked from binding to synthetic sialoside probes. Yet, despite the presence of cis ligands, CD22 redistributes to sites of cell contact by binding to trans ligands on neighboring cells. In this study, we demonstrate the dynamic equilibrium that exists between CD22 and its cis and trans ligands, using a high-affinity multivalent sialoside probe that competes with cis ligands and binds to CD22 on native human and murine B cells. Consistent with the constitutive endocytosis reported for CD22, the probes are internalized once bound, demonstrating that CD22 is an endocytic receptor that can carry ligand-decorated cargo to intracellular compartments. Conjugation of the sialoside probes to the toxin saporin resulted in toxin uptake and toxin-mediated killing of B lymphoma cell lines, suggesting an alternative approach for targeting CD22 for treatment of B cell lymphomas." @default.
• W2102321925 created "2016-06-24" @default.
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• W2102321925 creator A5072009532 @default.
• W2102321925 creator A5074812469 @default.
• W2102321925 date "2006-09-01" @default.
• W2102321925 modified "2023-10-03" @default.
• W2102321925 title "High-Affinity Ligand Probes of CD22 Overcome the Threshold Set by <i>cis</i> Ligands to Allow for Binding, Endocytosis, and Killing of B Cells" @default.
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• W2102321925 doi "https://doi.org/10.4049/jimmunol.177.5.2994" @default.
• W2102321925 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16920935" @default.
• W2102321925 hasPublicationYear "2006" @default.
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