Homomultimeric complexes of CD22 in B cells revealed by protein-glycan cross-linking

[1] Cyster JG(1997)Tuning antigen receptor signaling by CD22: integrating cues from antigens and the microenvironment Immunity 6 509-517

[2] Goodnow CC(1995)Characterization of sialyloligosaccharide binding by recombinant soluble and native cell-associated CD22. Evidence for a minimal structural recognition motif and the potential importance of multisite binding J. Biol. Chem. 270 7523-7532

[3] Powell LD(1998)Masking and unmasking of the sialic acid-binding lectin activity of CD22 (Siglec-2) on B lymphocytes Proc. Natl. Acad. Sci. USA 95 7469-7474

[4] Jain RK(2002)Sialic acid binding domains of CD22 are required for negative regulation of B cell receptor signaling J. Exp. Med. 195 1199-1205

[5] Matta KL(2002)The ligand-binding domain of CD22 is needed for inhibition of the B cell receptor signal, as demonstrated by a novel human CD22-specific inhibitor compound J. Exp. Med. 195 1207-1213

[6] Sabesan S(2004)CD22 regulates B lymphocyte function in vivo through both ligand-dependent and ligand-independent mechanisms Nat. Immunol. 5 1078-1087

[7] Varki A(1993)CD22, a B cell-specific immunoglobulin superfamily member, is a sialic acid-binding lectin J. Biol. Chem. 268 7011-7018

[8] Razi N(1995)Binding of human plasma sialoglycoproteins by the B cell-specific lectin CD22. Selective recognition of immunoglobulin M and haptoglobin J. Biol. Chem. 270 7543-7550

[9] Varki A(2004)Cell surface sialic acids do not affect primary CD22 interactions with CD45 and surface IgM nor the rate of constitutive CD22 endocytosis Glycobiology 14 939-949

[10] Jin L(2002)Versatile biosynthetic engineering of sialic acid in living cells using synthetic sialic acid analogues J. Biol. Chem. 277 6688-6695

[1] Cyster JG(1997)Tuning antigen receptor signaling by CD22: integrating cues from antigens and the microenvironment Immunity 6 509-517

[2] Goodnow CC(1995)Characterization of sialyloligosaccharide binding by recombinant soluble and native cell-associated CD22. Evidence for a minimal structural recognition motif and the potential importance of multisite binding J. Biol. Chem. 270 7523-7532

[3] Powell LD(1998)Masking and unmasking of the sialic acid-binding lectin activity of CD22 (Siglec-2) on B lymphocytes Proc. Natl. Acad. Sci. USA 95 7469-7474

[4] Jain RK(2002)Sialic acid binding domains of CD22 are required for negative regulation of B cell receptor signaling J. Exp. Med. 195 1199-1205

[5] Matta KL(2002)The ligand-binding domain of CD22 is needed for inhibition of the B cell receptor signal, as demonstrated by a novel human CD22-specific inhibitor compound J. Exp. Med. 195 1207-1213

[6] Sabesan S(2004)CD22 regulates B lymphocyte function in vivo through both ligand-dependent and ligand-independent mechanisms Nat. Immunol. 5 1078-1087

[7] Varki A(1993)CD22, a B cell-specific immunoglobulin superfamily member, is a sialic acid-binding lectin J. Biol. Chem. 268 7011-7018

[8] Razi N(1995)Binding of human plasma sialoglycoproteins by the B cell-specific lectin CD22. Selective recognition of immunoglobulin M and haptoglobin J. Biol. Chem. 270 7543-7550

[9] Varki A(2004)Cell surface sialic acids do not affect primary CD22 interactions with CD45 and surface IgM nor the rate of constitutive CD22 endocytosis Glycobiology 14 939-949

[10] Jin L(2002)Versatile biosynthetic engineering of sialic acid in living cells using synthetic sialic acid analogues J. Biol. Chem. 277 6688-6695