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The extent of glycan processing is surprising considering the position of the J chain within the center of the IgM pentamer (Figure 5). IgM μ-chain mainly contains monosialylated bi-antennary structures (Table 1), suggesting that crowding may prevent the glycosylation machinery from processing all 30 complex N-linked gly- Annu. Rev. Immunol. 25:21-50. org by HINARI on 08/26/07. For personal use only. ANRV306-IY25-02 32 Arnold et al. cans per pentamer to disialylated structures. Possibly the J chain is more flexible as it links the C-termini of the tailpieces of two IgM μchains.

Rudd PM, Elliott T, Cresswell P, Wilson IA, Dwek RA. 2001. Glycosylation and the immune system. Science 291:2370–76 9. Bergeron JJ, Brenner MB, Thomas DY, Williams DB. 1994. Calnexin: a membranebound chaperone of the endoplasmic reticulum. Trends Biochem. Sci. 19:124–28 10. Scanlan CN, Pantophlet R, Wormald MR, Ollmann Saphire E, Stanfield R, et al. 2002. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1→2 mannose residues on the outer face of gp120.

Structural and functional analysis of J chain-deficient IgM. J. Immunol. 160:5979–89 46. Norderhaug IN, Johansen FE, Schjerven H, Brandtzaeg P. 1999. Regulation of the formation and external transport of secretory immunoglobulins. Crit. Rev. Immunol. 19:481–508 47. Lamm ME. 1997. Interaction of antigens and antibodies at mucosal surfaces. Annu. Rev. Microbiol. 51:311–40 48. Mantis NJ, Farrant SA, Mehta S. 2004. Oligosaccharide side chains on human secretory IgA serve as receptors for ricin. J. Immunol.

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