Structure of the oligosaccharide of human J chain.

Baenziger, Jacques U.

doi:10.1016/s0021-9258(18)50696-7

Cited by 45 publications

(2 citation statements)

References 45 publications

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“…There is a conserved N -glycosylation site at Asn49 of the human J-chain. The attached oligosaccharides are represented in three forms, each differing in the amount of sialic acid, 30% contain two sialic acid residues, 55% contain a sialic acid residue on the α l,3-linked mannose branch, and 15% have no sialic acid but two terminal galactose residues [ 55 ]. The glycosylated murine J-chain mutant with an Asn48 (corresponding to Asn49 of human J-chain) to Ala substitution in human IgA1 has reduced dimer assembly [ 56 ].…”

Section: Structure Of J-chainmentioning

confidence: 99%

3D Structures of IgA, IgM, and Components

Pan

Manabe

Yamaguchi

2021

IJMS

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Immunoglobulin G (IgG) is currently the most studied immunoglobin class and is frequently used in antibody therapeutics in which its beneficial effector functions are exploited. IgG is composed of two heavy chains and two light chains, forming the basic antibody monomeric unit. In contrast, immunoglobulin A (IgA) and immunoglobulin M (IgM) are usually assembled into dimers or pentamers with the contribution of joining (J)-chains, which bind to the secretory component (SC) of the polymeric Ig receptor (pIgR) and are transported to the mucosal surface. IgA and IgM play a pivotal role in various immune responses, especially in mucosal immunity. Due to their structural complexity, 3D structural study of these molecules at atomic scale has been slow. With the emergence of cryo-EM and X-ray crystallographic techniques and the growing interest in the structure-function relationships of IgA and IgM, atomic-scale structural information on IgA-Fc and IgM-Fc has been accumulating. Here, we examine the 3D structures of IgA and IgM, including the J-chain and SC. Disulfide bridging and N-glycosylation on these molecules are also summarized. With the increasing information of structure–function relationships, IgA- and IgM-based monoclonal antibodies will be an effective option in the therapeutic field.

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Section: Structure Of J-chainmentioning

confidence: 99%

3D Structures of IgA, IgM, and Components

Pan

Manabe

Yamaguchi

2021

IJMS

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“…Immunoglobulin A and SIgA are heavily glycosylated proteins with oligosaccharide side chains accounting for >10% of the molecular mass of the IgA H chain (Tomana et al, 1976), 8% of the J-chain (Baenziger, 1979;Royle et al, 2003), and 15-20% of SC (Hughes et al, 1999;Phalipon et al, 2002). The presence or absence of glycans as well as their structure can affect IgA assembly, secretion, and function.…”

Section: Role Of Carbohydrates In Iga and Sigamentioning

confidence: 99%

Recombinant IgA Antibodies

Yoo

Chintalacharuvu

Morrison

2007

Mucosal Immune Defense: Immunoglobulin A

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Site‐specific analysis of the N‐glycans on murine polymeric immunoglobulin A using liquid chromatography/electrospray mass spectrometry

et al. 1995

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The site-specific distribution of oligosaccharides on murine polymeric immunoglobulin A (pIgA) consisting of two or more immunoglobulin A (IgA) antibodies connected through J-chain was analysed by liquid chromatographylelectrospray mass spectrometry. Glycopeptides from pIgA were localized in a reversed-phase tryptic peptide chromatogram by collision excitation scanning and their amino acid sequences determined by electrospray tandem mass spectrometry and Edman degradation. Two glycosylation sites on IgA and a single glycosylation site on J-chain were identified. Using biosynthetic constraints on carbohydrate structures, molecular mass information on the glycan moieties of the glycopeptides was translated into specific carbohydrate structure proposals. The glycopeptide incorporating the single glycosylation site at Am49 in J-chain carried fucosylated and non-fucosylated di-and triantennary N-acetyllactosamine type carbohydrate chains terminated by N-acetyl-and/or Nglycolylneuraminic acid residues. The glycosylation site in the IgA heavy chain at Asn446 contained two oligomannose-type carbohydrate chains, one carrying five and the other six mannose residues. To the other glycosylation site in the IgA heavy chain at A d 5 5 one oligomannose structure, hybrid structures with the lactosamine branch terminated by either an additional galactose residue, N-glycolylneuraminic acid or N-acetylneuraminic acid, and non-fucosylated N-acetyllactosamine-type structures carrying the same terminating residues were attached. This glycosylation site was present in two separate glycopeptides differing only in their degree of carboxymethylation and yielding identical oligosaccharide distributions, thus providing additional confidence in the assignment method.

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Structure of the oligosaccharide of human J chain.

Cited by 45 publications

References 45 publications

3D Structures of IgA, IgM, and Components

3D Structures of IgA, IgM, and Components

Recombinant IgA Antibodies

Site‐specific analysis of the N‐glycans on murine polymeric immunoglobulin A using liquid chromatography/electrospray mass spectrometry

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