Molecular basis of human CD22 function and therapeutic targeting
Abstract
CD22 maintains a baseline level of B-cell inhibition to keep humoral immunity in check. As a B-cell-restricted antigen, CD22 is targeted in therapies against dysregulated B cells that cause autoimmune diseases and blood cancers. Here we report the crystal structure of human CD22 at 2.1 Å resolution, which reveals that specificity for α2-6 sialic acid ligands is dictated by a pre-formed β-hairpin as a unique mode of recognition across sialic acid-binding immunoglobulin-type lectins. The CD22 ectodomain adopts an extended conformation that facilitates concomitant CD22 nanocluster formation on B cells and binding to trans ligands to avert autoimmunity in mammals. We structurally delineate the CD22 site targeted by the therapeutic antibody epratuzumab at 3.1 Å resolution and determine a critical role for CD22 N-linked glycosylation in antibody engagement. Our studies provide molecular insights into mechanisms governing B-cell inhibition and valuable clues for the design of immune modulators in B-cell dysfunction.
- Authors:
-
- The Hospital for Sick Children Research Inst., Toronto, ON (Canada)
- The Hospital for Sick Children Research Inst., Toronto, ON (Canada); Univ. of Toronto, ON (Canada)
- McMaster Univ., Hamilton, ON (Canada)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division; Canadian Inst. of Health Research
- OSTI Identifier:
- 1432854
- Grant/Contract Number:
- AC02-06CH11357; PJT-148811
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 8; Journal Issue: 1; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Electron microscopy; Immunology; SAXS; X-ray crystallography
Citation Formats
Ereño-Orbea, June, Sicard, Taylor, Cui, Hong, Mazhab-Jafari, Mohammad T., Benlekbir, Samir, Guarné, Alba, Rubinstein, John L., and Julien, Jean-Philippe. Molecular basis of human CD22 function and therapeutic targeting. United States: N. p., 2017.
Web. doi:10.1038/s41467-017-00836-6.
Ereño-Orbea, June, Sicard, Taylor, Cui, Hong, Mazhab-Jafari, Mohammad T., Benlekbir, Samir, Guarné, Alba, Rubinstein, John L., & Julien, Jean-Philippe. Molecular basis of human CD22 function and therapeutic targeting. United States. https://doi.org/10.1038/s41467-017-00836-6
Ereño-Orbea, June, Sicard, Taylor, Cui, Hong, Mazhab-Jafari, Mohammad T., Benlekbir, Samir, Guarné, Alba, Rubinstein, John L., and Julien, Jean-Philippe. Mon .
"Molecular basis of human CD22 function and therapeutic targeting". United States. https://doi.org/10.1038/s41467-017-00836-6. https://www.osti.gov/servlets/purl/1432854.
@article{osti_1432854,
title = {Molecular basis of human CD22 function and therapeutic targeting},
author = {Ereño-Orbea, June and Sicard, Taylor and Cui, Hong and Mazhab-Jafari, Mohammad T. and Benlekbir, Samir and Guarné, Alba and Rubinstein, John L. and Julien, Jean-Philippe},
abstractNote = {CD22 maintains a baseline level of B-cell inhibition to keep humoral immunity in check. As a B-cell-restricted antigen, CD22 is targeted in therapies against dysregulated B cells that cause autoimmune diseases and blood cancers. Here we report the crystal structure of human CD22 at 2.1 Å resolution, which reveals that specificity for α2-6 sialic acid ligands is dictated by a pre-formed β-hairpin as a unique mode of recognition across sialic acid-binding immunoglobulin-type lectins. The CD22 ectodomain adopts an extended conformation that facilitates concomitant CD22 nanocluster formation on B cells and binding to trans ligands to avert autoimmunity in mammals. We structurally delineate the CD22 site targeted by the therapeutic antibody epratuzumab at 3.1 Å resolution and determine a critical role for CD22 N-linked glycosylation in antibody engagement. Our studies provide molecular insights into mechanisms governing B-cell inhibition and valuable clues for the design of immune modulators in B-cell dysfunction.},
doi = {10.1038/s41467-017-00836-6},
journal = {Nature Communications},
number = 1,
volume = 8,
place = {United States},
year = {Mon Oct 02 00:00:00 EDT 2017},
month = {Mon Oct 02 00:00:00 EDT 2017}
}
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