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Serum IgA glycans bind ASGP-R. Serum IgA consists mainly of IgA1 and circulates at around 1 mg/ml, and, although it is predominantly monomeric (Figure 4), it also forms dimers and higher polymers (35, 36). The glycosylation of IgA has been widely reported (37–40) (Table 1). The galactose-terminating glycans are ligands for the asialoglycoprotein receptor (ASGP-R), which mediates the clearance of IgA from the serum (41, 42). Thirty percent of serum IgA contains N-linked glycans attached to glycosylation sites in the Fab variable regions of the α- and LCs (38).

75:591–609 43. Johansen FE, Braathen R, Brandtzaeg P. 2001. The J chain is essential for polymeric Ig receptor-mediated epithelial transport of IgA. J. Immunol. 167:5185–92 44. Royle L, Roos A, Harvey DJ, Wormald MR, van Gijlswijk-Janssen D, et al. 2003. Secretory IgA N- and O-glycans provide a link between the innate and adaptive immune systems. J. Biol. Chem. 278:20140–53 45. Wiersma EJ, Collins C, Fazel S, Shulman MJ. 1998. Structural and functional analysis of J chain-deficient IgM. J. Immunol.

Schroten H, Stapper C, Plogmann R, Kohler H, Hacker J, Hanisch FG. 1998. Fabindependent antiadhesion effects of secretory immunoglobulin A on S-fimbriated Escherichia coli are mediated by sialyloligosaccharides. Infect. Immun. 66:3971–73 50. Wold AE, Mestecky J, Tomana M, Kobata A, Ohbayashi H, et al. 1990. Secretory immunoglobulin A carries oligosaccharide receptors for Escherichia coli type 1 fimbrial lectin. Infect. Immun. 58:3073–77 51. Krugmann S, Pleass RJ, Atkin JD, Woof JM. 1997. Mutagenesis of J chain residues critical for IgA dimer assembly.

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