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Structure paper

TitleMolecular basis of human CD22 function and therapeutic targeting.
Journal, issue, pagesNat Commun, Vol. 8, Issue 1, Page 764, Year 2017
Publish dateOct 2, 2017
AuthorsJune Ereño-Orbea / Taylor Sicard / Hong Cui / Mohammad T Mazhab-Jafari / Samir Benlekbir / Alba Guarné / John L Rubinstein / Jean-Philippe Julien /
PubMed AbstractCD22 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 ...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.The B-cell-specific co-receptor CD22 is a therapeutic target for depleting dysregulated B cells. Here the authors structurally characterize the ectodomain of CD22 and present its crystal structure with the bound therapeutic antibody epratuzumab, which gives insights into the mechanism of inhibition of B-cell activation.
External linksNat Commun / PubMed:28970495 / PubMed Central
MethodsSAS (X-ray synchrotron) / EM (single particle) / X-ray diffraction
Resolution2.014 - 30.0 Å
Structure data

SASDC76:
Extracellular domain of human B-lymphocyte cell receptor CD22
Method: SAXS/SANS

SASDC86:
Extracellular domain of human B-lymphocyte cell receptor CD22 in complex with alpha 2,6 sialyllactose
Method: SAXS/SANS

EMDB-8704:
Negative stain electron microscopy map of human CD22 extracellular domain
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-8705:
Negative stain electron microscopy map of human CD22 extracellular domain in complex with epratuzumab Fab
Method: EM (single particle) / Resolution: 30.0 Å

PDB-5vkj:
Crystal structure of human CD22 Ig domains 1-3
Method: X-RAY DIFFRACTION / Resolution: 2.12 Å

PDB-5vkk:
Crystal structure of Fab fragment of anti-CD22 Epratuzumab
Method: X-RAY DIFFRACTION / Resolution: 2.014 Å

PDB-5vkm:
Crystal structure of human CD22 Ig domains 1-3 in complex with alpha 2-6 sialyllactose
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-5vl3:
CD22 d1-d3 in complex with therapeutic Fab Epratuzumab
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsIMMUNE SYSTEM / Siglec / Sialic acid / carbohydrate binding protein / therapeutic antibody / B cell / Fab

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