Phylogeny and Comparative Physiology of Mucosal Immunoglobulins

Kaetzel, Charlotte S.; Russell, Michael W.

doi:10.1016/b978-0-12-415847-4.00018-5

Cited by 7 publications

(12 citation statements)

References 210 publications

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“…The most striking difference in the HR of α1 and α2 H chains is in the insertion of 13 amino-acid residues in HR of α1 H chains. A detailed comparison of human, chimpanzee, and gorilla IgA HRs with IgA HRs of 10 other species (including 13 subclasses of lagomorphs’ IgA) clearly demonstrates the structural uniqueness of human and hominoid primate IgA1 [13–15]. Due to the duplicated octapeptide with Pro, Ser, and Thr residues and the Ser/Thr-attached glycans, the HR of IgA1 is reminiscent of that of mucin glycopeptides with O -glycans.…”

Section: Why Iga1?mentioning

confidence: 99%

“…Therefore, the putative antigen, Gal-deficient HR glycan essential for the formation of IC is absent. Moreover, the IgA systems in humans and experimental animals display marked differences in the dominant molecular forms, biosynthesis, catabolism and transport [15]. In contrast to humans, almost all IgA in the murine circulation is present in the polymeric form and is effectively removed either in the free form or as IC from the circulation by the pIgR expressed on hepatocytes, which thus participate in the hepatobiliary transport [15].…”

Section: How Useful Are Animal Models Of Igan?mentioning

confidence: 99%

“…Moreover, the IgA systems in humans and experimental animals display marked differences in the dominant molecular forms, biosynthesis, catabolism and transport [15]. In contrast to humans, almost all IgA in the murine circulation is present in the polymeric form and is effectively removed either in the free form or as IC from the circulation by the pIgR expressed on hepatocytes, which thus participate in the hepatobiliary transport [15]. However, murine models may be useful in assessing some aspects of IgAN, including the testing of various inhibitors of immune-complex formation or activity (for review, see [12]).…”

Section: How Useful Are Animal Models Of Igan?mentioning

confidence: 99%

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IgA nephropathy enigma

Městecký

Novák

Moldoveanu

et al. 2016

Clinical Immunology

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IgA nephropathy (IgAN) is the leading cause of primary glomerulonephritis in the world. The disease is characterized by the presence of immune complexes in the circulation and in mesangial deposits with ensuing glomerular injury. Although in humans there are two IgA subclasses, only IgA1 molecules are involved. The exclusivity of participation of IgA1 in IgAN prompted extensive structural and immunological studies of the unique hinge region (HR) of IgA1, which is absent in otherwise highly homologous IgA2. HR of IgA1 with altered O-glycans serves as an antigen recognized by autoantibodies specific for aberrant HR glycans leading to the generation of nephritogenic immune complexes. However, there are several unresolved questions concerning the phylogenetic origin of human IgA1 HR, the structural basis of its antigenicity, the origin of antibodies specific for HR with altered glycan moieties, the regulatory defects in IgA1 glycosylation pathways, and the potential approaches applicable to the disease-specific interventions in the formation of nephritogenic immune complexes. This review focuses on the gaps in our knowledge of molecular and cellular events that are involved in the immunopathogenesis of IgAN.

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Section: Why Iga1?mentioning

confidence: 99%

Section: How Useful Are Animal Models Of Igan?mentioning

confidence: 99%

Section: How Useful Are Animal Models Of Igan?mentioning

confidence: 99%

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IgA nephropathy enigma

Městecký

Novák

Moldoveanu

et al. 2016

Clinical Immunology

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“…The structure of Ig genes and their encoded proteins has been studied extensively in extant species of the class Mammalia, including the egg-laying monotremes, the pouch-bearing marsupials, and the placentals (eutherians) (reviewed in [8]). The IGH locus in all known mammals is organized as a translocon with gene segments encoding IgM, IgD, 2 or more subclasses of IgG, 1 or more subclasses of IgA, and IgE, an isotype unique to mammals ( Figure 1).…”

Section: Mammalsmentioning

confidence: 99%

“…Some Ig isotypes can form higher-order polymers of the basic 4-chain unit, thus increasing the number of Ag-binding sites and enhancing Fc-mediated functions. The emergence of new Ig isotypes during vertebrate evolution allowed for diversification of Ig-mediated immune functions, including those specialized for mucosal surfaces (reviewed in [8]). Many Ig-mediated immune functions involve interactions with isotype-specific cellular receptors for the Fc region of Ig heavy chains ( Figure 3).…”

Section: Introductionmentioning

confidence: 99%

Coevolution of Mucosal Immunoglobulins and the Polymeric Immunoglobulin Receptor: Evidence That the Commensal Microbiota Provided the Driving Force

Kaetzel

2014

ISRN Immunology

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Immunoglobulins (Igs) in mucosal secretions contribute to immune homeostasis by limiting access of microbial and environmental antigens to the body proper, maintaining the integrity of the epithelial barrier and shaping the composition of the commensal microbiota. The emergence of IgM in cartilaginous fish represented the primordial mucosal Ig, which is expressed in all higher vertebrates. Expansion and diversification of the mucosal Ig repertoire led to the emergence of IgT in bony fishes, IgX in amphibians, and IgA in reptiles, birds, and mammals. Parallel evolution of cellular receptors for the constant (Fc) regions of Igs provided mechanisms for their transport and immune effector functions. The most ancient of these Fc receptors is the polymeric Ig receptor (pIgR), which first appeared in an ancestor of bony fishes. The pIgR transports polymeric IgM, IgT, IgX, and IgA across epithelial cells into external secretions. Diversification and refinement of the structure of mucosal Igs during tetrapod evolution were paralleled by structural changes in pIgR, culminating in the multifunctional secretory IgA complex in mammals. In this paper, evidence is presented that the mutualistic relationship between the commensal microbiota and the vertebrate host provided the driving force for coevolution of mucosal Igs and pIgR.

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Easy pan-detection of human IgA immunoglobulins

Planchais

Mouquet

2020

Journal of Immunological Methods

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Phylogeny and Comparative Physiology of Mucosal Immunoglobulins

Cited by 7 publications

References 210 publications

IgA nephropathy enigma

IgA nephropathy enigma

Coevolution of Mucosal Immunoglobulins and the Polymeric Immunoglobulin Receptor: Evidence That the Commensal Microbiota Provided the Driving Force

Easy pan-detection of human IgA immunoglobulins

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