Lack of SC/pIgR‐mediated epithelial transport of a human polymeric IgA devoid of J chain: <i>in vitro</i> and <i>in vivo</i> studies

Vaerman, Jean‐Pierre; Langendries, Agnès; Giffroy, D; Brandtzæg, Per; Kobayashi, Kunihiko

doi:10.1046/j.1365-2567.1998.00560.x

Cited by 41 publications

(28 citation statements)

References 33 publications

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“…The doublet band at ϳ31 kDa corresponds to L chains and to the J chain, as shown with specific Abs (data not shown). Although the J chain has a calculated molecular mass of 15-16 kDa, it migrated more slowly than expected, as previously observed (51,54,55).…”

Section: Purification Of S-igasupporting

confidence: 82%

Isolation and Detection of Human IgA Using a Streptococcal IgA-Binding Peptide

Sandin

Linse

Areschoug

et al. 2002

The Journal of Immunology

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Bacterial proteins that bind to the Fc part of IgG have found widespread use in immunology. A similar protein suitable for the isolation and detection of human IgA has not been described. Here, we show that a 50-residue synthetic peptide, designated streptococcal IgA-binding peptide (Sap) and derived from a streptococcal M protein, can be used for single-step affinity purification of human IgA. High affinity binding of IgA required the presence in Sap of a C-terminal cysteine residue, not present in the intact M protein. Passage of human serum through a Sap column caused depletion of >99% of the IgA, and elution of the column allowed quantitative recovery of highly purified IgA, for which the proportions of the IgA1 and IgA2 subclasses were the same as in whole serum. Moreover, immobilized Sap could be used for single-step purification of secretory IgA of both subclasses from human saliva, with a recovery of ∼45%. The Sap peptide could also be used to specifically detect IgA bound to Ag. Together, these data indicate that Sap is a versatile Fc-binding reagent that may open new possibilities for the characterization of human IgA.

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Section: Purification Of S-igasupporting

confidence: 82%

Isolation and Detection of Human IgA Using a Streptococcal IgA-Binding Peptide

Sandin

Linse

Areschoug

et al. 2002

The Journal of Immunology

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“…Cys 467 on domain V of the secretory component forms a disulfide bond with Cys 311 on the C␣2 domain of one of the IgA1 monomers (55), which fixes its position. In addition, residues on domain I of the SC have been shown to interact with the J chain (56) and one of the C␣3 domains (57,58). This has been modeled as the secretory component wrapping around the IgA1/J chain complex, so that domain V is bonded to one IgA1 monomer and domain I interacts with the other monomer.…”

Section: Fig 5 Np Hplc Profiles Of N-glycans From H Chains Of Siga1mentioning

confidence: 99%

“…J Chain Conformation Requires an N-glycan-The J chain on dimeric IgA is essential for binding to pIgR and translocation across the epithelial cells (2,56). Deletion of the N-glycan site, by substitution of Asn with alanine, prevents IgA dimer formation (54), indicating that the N-glycan plays an important role in this process.…”

Section: N-glycans Of Sc Present Many Epitopes For Bacterial Adhesin mentioning

confidence: 99%

Secretory IgA N- and O-Glycans Provide a Link between the Innate and Adaptive Immune Systems

Royle

Roos

Harvey

et al. 2003

Journal of Biological Chemistry

301

327

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Secretory IgA (SIgA) is a multi-polypeptide complex consisting of a secretory component (SC) covalently attached to dimeric IgA containing one joining (J) chain. We present the analysis of both the N-and O-glycans on the individual peptides from this complex. Based on these data, we have constructed a molecular model of SIgA1 with all its glycans, in which the Fab arms form a T shape and the SC is wrapped around the heavy chains. The O-glycan regions on the heavy (H) chains and the SC N-glycans have adhesin-binding glycan epitopes including galactose-linked ␤1-4 and ␤1-3 to GlcNAc, fucoselinked ␣1-3 and ␣1-4 to GlcNAc and ␣1-2 to galactose, and ␣2-3 and ␣2-6-linked sialic acids. These glycan epitopes provide SIgA with further bacteria-binding sites in addition to the four Fab-binding sites, thus enabling SIgA to participate in both innate and adaptive immunity. We also show that the N-glycans on the H chains of both SIgA1 and SIgA2 present terminal GlcNAc and mannose residues that are normally masked by SC, but that can be unmasked and recognized by mannosebinding lectin, by disrupting the SC-H chain noncovalent interactions.

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“…This J-chain includes cysteine residues implicated in IgA (and IgM) polymerization, and is necessary for the transepithelial transport of pIgs. More specifically, the J-chain is not mandatory for polymer formation, but regulates their quaternary structure ("tail-to-tail" model for IgA and ring structure for IgM), which appears to be a determinant for the binding to the epithelial pIgR [11][12][13]. pIgA is mainly represented by dimeric IgA (335 kDa and 9.5S), whereas higher aggregation states (trimers and tetramers) are also found, usually in smaller proportions.…”

Section: Organization Of the Mucosal Immunoglobulin-a Systemmentioning

confidence: 99%

Lung mucosal immunity: immunoglobulin-A revisited

et al. 2001

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Mucosal defence mechanisms are critical in preventing colonization of the respiratory tract by pathogens and penetration of antigens through the epithelial barrier. Recent research has now illustrated the active contribution of the respiratory epithelium to the exclusion of microbes and particles, but also to the control of the inflammatory and immune responses in the airways and in the alveoli. Epithelial cells also mediate the active transport of polymeric immunoglobulin-A from the lamina propria to the airway lumen through the polymeric immunoglobulin receptor. The role of IgA in the defence of mucosal surfaces has now expanded from a limited role of scavenger of exogenous material to a broader protective function with potential applications in immunotherapy. In addition, the recent identification of receptors for IgA on the surface of blood leukocytes and alveolar macrophages provides an additional mechanism of interaction between the cellular and humoral immune systems at the level of the respiratory tract.

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Lack of SC/pIgR‐mediated epithelial transport of a human polymeric IgA devoid of J chain: in vitro and in vivo studies

Cited by 41 publications

References 33 publications

Isolation and Detection of Human IgA Using a Streptococcal IgA-Binding Peptide

Isolation and Detection of Human IgA Using a Streptococcal IgA-Binding Peptide

Secretory IgA N- and O-Glycans Provide a Link between the Innate and Adaptive Immune Systems

Lung mucosal immunity: immunoglobulin-A revisited

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