Artiodactyl IgD: The Missing Link

Zhao, Yaofeng; Kacskovıcs, Imre; Pan, Qiang; Liberles, David A.; Geli, János; Davis, Scott K.; Rabbani, Hodjattallah; Hammarström, Lennart

doi:10.4049/jimmunol.169.8.4408

Cited by 95 publications

(103 citation statements)

References 36 publications

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“…IgD has previously been found only in mammals and fish but not in birds and amphibians (6,27). The discovery of IgD in X. tropicalis partially fills this evolutionary gap.…”

Section: Discussionmentioning

confidence: 79%

“…Mammalian IgM and IgE heavy chains are composed of four Ϸ110-aa constant region domains encoded by separate exons, presumably arising from gene duplication during evolution (3). IgD and IgG contain only three domains (rodent IgD contains only two constant region domains) but also encompass a short exon-encoded hinge (genetic hinge) (4)(5)(6)(7). IgA is also a three-domain molecule, with a functional hinge encoded by the 5Ј end of the heavy-chain constant region domain (C H ) 2 (C H 2) exon (8,9).…”

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confidence: 99%

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Identification of IgF, a hinge-region-containing Ig class, and IgD inXenopus tropicalis

Zhao

Pan‐Hammarström

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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103

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Only three Ig isotypes, IgM, IgX, and IgY, were previously known in amphibians. Here, we describe a heavy-chain isotype in Xenopus tropicalis, IgF (encoded by C ), with only two constant region domains. IgF is similar to amphibian IgY in sequence, but the gene contains a hinge exon, making it the earliest example, in evolution, of an Ig isotype with a separately encoded genetic hinge. We also characterized a gene for the heavy chain of IgD, located immediately 3 of C , that shares features with the C␦ gene in fish and mammals. The latter gene contains eight constant-region-encoding exons and, unlike the chimeric splicing of CH1 onto the IgD heavy chain in teleost fish, it is expressed as a unique IgD heavy chain. The IgH locus of X. tropicalis shows a 5 V H-DH-JH-C -C␦-C -C -C 3 organization, suggesting that the mammalian and amphibian Ig heavy-chain loci share a common ancestor.amphibians ͉ antibody evolution

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“…IgD has previously been found only in mammals and fish but not in birds and amphibians (6,27). The discovery of IgD in X. tropicalis partially fills this evolutionary gap.…”

Section: Discussionmentioning

confidence: 79%

mentioning

confidence: 99%

Identification of IgF, a hinge-region-containing Ig class, and IgD inXenopus tropicalis

Zhao

Pan‐Hammarström

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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103

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“…In mammals, there are different numbers of C domains in different species, even between mouse and human (27). In artiodactyl species (pig, sheep, and cow), the ␦1 domain-encoding exon has been deleted and replaced with a duplicated 1 exon (8,35,36), and the ␦ gene has been dispensed with altogether in chicken and rabbit (ref. 37 and unpublished observations).…”

Section: Discussionmentioning

confidence: 99%

IgD, like IgM, is a primordial immunoglobulin class perpetuated in most jawed vertebrates

Ohta

Flajnik²

2006

Proc. Natl. Acad. Sci. U.S.A.

196

138

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IgD has remained a mysterious Ig class and a bane to immunology students since its discovery >40 years ago. Its spotty occurrence in mammals and birds and the discovery of an isotype with similarities to IgD in bony fish are perplexing. We have identified IgD heavy (H) chain (␦) from the amphibian Xenopus tropicalis during examination of the IgH locus. The Xenopus ␦ gene is in the same position, immediately 3 of the IgM gene, as in mammals, and it is expressed only in the spleen at low levels, primarily as a transmembrane receptor by surface IgM ؉ cells. Our data suggest that frog IgD is expressed on mature B cells, like in mouse͞human. Unexpectedly, Xenopus IgD is orthologous to IgW, an Ig isotype found only in cartilaginous fish and lungfish, demonstrating that IgD͞W, like IgM, was present in the ancestor of all living jawed vertebrates. In striking contrast to IgM, IgD͞W is evolutionarily labile, showing many duplications͞deletions of domains, the presence of multiple splice forms, existence as predominantly a secretory or transmembrane form, or loss of the entire gene in a species-specific manner. Our study suggests that IgD͞W has played varied roles in different vertebrate taxa since the inception of the adaptive immune system, and it may have been preserved as a flexible locus over evolutionary time to complement steadfast IgM.evolution ͉ immune system S ince the pioneering work of comparative immunologists in the 1960s, IgM has been the Ig isotype believed to be primordial and most stable in vertebrate evolution (1). Despite differences in the degree of polymerization of the secretory form in different vertebrate groups (1, 2) and a major splice variant of the transmembrane (TM) form in teleost fish (3), IgM is renowned for its molecular, biochemical, and functional stability. Present in all living jawed vertebrates, IgM is the first isotype to be expressed both in ontogeny and during humoral adaptive immune responses and is found as the major TM receptor on the surface of both conventional and ''innate'' B cells (4).By contrast, IgD has remained an enigmatic isotype since its discovery long ago (5). Like IgM, IgD is expressed as a TM receptor on B cells of mouse and human, generated as a result of alternative splicing of pre-mRNA containing the transcribed variable (V) region and the IgM and IgD heavy (H) chain constant (C) regions ( and ␦, respectively). Because of its spotty presence in mammals and absence in birds, IgD was assumed to be a recently evolved isotype (6). However, the discovery of an isotype in ray-finned bony fish with sequence similarity to IgD (7) and its presence in some mammals previously believed to lack IgD (8) have greatly modified our view of Ig isotype evolution and suggested it may have arisen much earlier.A similarly strange phylogenetic jump surrounds the isotype IgW, which was discovered first in skates (9, 10) and later in sharks (11,12). The secreted version of the IgW H chain ( ) is present in long and short forms in all elasmobranchs tested to date, and the TM form is al...

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“…The constant regions of bovine IgD, IgM, IgG1, IgG2, IgG3, IgE and IgA have been well characterized [16,52,69,70,94,111,121]. The constant regions identified in sheep are IgD, IgM (possibly two IgM allotypes), IgG1, IgG2, IgE and IgA [18,24,31,45,86,114,121].…”

Section: Molecular Mechanisms Of B-cell Diversity and Ig Isotypesmentioning

confidence: 99%

“…The constant regions identified in sheep are IgD, IgM (possibly two IgM allotypes), IgG1, IgG2, IgE and IgA [18,24,31,45,86,114,121].…”

Section: Molecular Mechanisms Of B-cell Diversity and Ig Isotypesmentioning

confidence: 99%

The sheep and cattle Peyer’s patch as a site of B-cell development

et al. 2006

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-In sheep and cattle, the ileal Peyer's patch (PP), which extends one-two meters along the terminal small intestine, is a primary lymphoid organ of B-cell development. B-cell diversity in the ileal PP is thought to develop by combinatorial mechanisms, gene conversion and/or point mutation. These species also have jejunal PP that function more like secondary lymphoid tissues concerned with mucosal immune reactions. These two types of PP differ significantly in their histology, ontogeny and the extent of lymphocyte traffic. The prenatal development of follicles in the PP begins first in the jejunum during the middle of gestation and then in the ileum during late gestation. B-cells proliferate rapidly in the ileal PP follicle; up to five percent of these cells survive while the majority dies by apoptosis, perhaps driven by the influence of environmental antigen and/ or self-antigen. The surviving cells migrate from the ileal PP and populate the peripheral B-cell compartment. By adolescence, the ileal PP has involuted but the function of jejunal PP, compatible with a role as secondary lymphoid organ, continues throughout life. In this review, we focus on the development of PP as a site of B-cell repertoire generation, positive and negative B-cell selection, and the differences between ileal PP and jejunal PP.

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Artiodactyl IgD: The Missing Link

Cited by 95 publications

References 36 publications

Identification of IgF, a hinge-region-containing Ig class, and IgD inXenopus tropicalis

Identification of IgF, a hinge-region-containing Ig class, and IgD inXenopus tropicalis

IgD, like IgM, is a primordial immunoglobulin class perpetuated in most jawed vertebrates

The sheep and cattle Peyer’s patch as a site of B-cell development

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