Cloning of IgE from the echidna (Tachyglossus aculeatus) and a comparative analysis of ε chains from all three extant mammalian lineages

Vernersson, Molly; Aveskogh, Maria; Hellman, Lars

doi:10.1016/s0145-305x(03)00084-3

Cited by 54 publications

(39 citation statements)

References 59 publications

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“…In the mIgE + B cells, *100 times more transcripts for se than for me were found. In contrast, in mIgG 1 + B cells, *140 times more transcripts for mc 1 than for sc 1 were found. Thus, the expression pattern of both mRNA and protein of se and me reflects the variant structure of the 3 0 UTR of the e gene and is different from that of the other Ig classes.…”

Section: Introductionmentioning

confidence: 77%

“…Total RNA was extracted from the two cell populations and reverse transcribed (Superscipt II; Invitrogen) using oligo-dT as primer for first-strand synthesis. Quantitative determination of transcripts for se and me and for sc 1 and mc 1 was performed by PCR using the LightCycler instrument (Roche) according to protocols supplied by the manufacturer.…”

Section: Isolation Of Cellsmentioning

confidence: 99%

“…However, the prime target for IgE is still unknown. From an evolutionary point of view, IgE is conserved and can be found in all mammalia, including monotremata [1]. It therefore originated at least 160 million years ago, possibly even more than 300 million years ago [2], from a gene duplication of IgY, in which the anaphylactic and opsonic activities of IgY were separated, giving rise to IgE and IgG, respectively [3].…”

Section: Introductionmentioning

confidence: 99%

“…Spleen cells from CD23-deficient mice were stimulated for 4 days with LPS and IL-4 and then stained with antibodies to the pan-B cell marker B220, IgE and IgG 1 . mIgE + and mIgG 1 + B cells were isolated by cell sorting (Fig.…”

Section: Introductionmentioning

confidence: 99%

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Inefficient processing of mRNA for the membraneform of IgE is a genetic mechanism to limit recruitment of IgE‐secreting cells

et al. 2006

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Immunoglobulin E (IgE) is the key effector element in allergic diseases ranging from innocuous hay fever to life-threatening anaphylactic shock. Compared to other Ig classes, IgE serum levels are very low. In its membrane-bound form (mIgE), IgE behaves as a classical antigen receptor on B lymphocytes. Expression of mIgE is essential for subsequent recruitment of IgE-secreting cells. We show that in activated, mIgE-bearing B cells, mRNA for the membrane forms of both murine and human epsilon (e) heavy chains (HC) are poorly expressed compared to mRNA for the secreted forms. In contrast, in mIgG-bearing B cells, mRNA for the membrane forms of murine gamma-1 (c1) and the corresponding human c4 HC are expressed at a much higher level than mRNA for the respective secreted forms. We show that these findings correlate with the presence of deviant polyadenylation signal hexamers in the 3 0 untranslated region (UTR) of both murine and human e genes, causing inefficient processing of primary transcripts and thus poor expression of the proteins and poor recruitment of IgEproducing cells in the immune response. Thus, we have identified a genetic steering mechanism in the regulation of IgE synthesis that represents a further means to restrain potentially dangerous, high serum IgE levels.

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Section: Introductionmentioning

confidence: 77%

Section: Isolation Of Cellsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Inefficient processing of mRNA for the membraneform of IgE is a genetic mechanism to limit recruitment of IgE‐secreting cells

et al. 2006

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“…It is clear from sequence comparisons that after the divergence of the synapsids 310 million years ago (16,17), but before the divergence of the non-eutherian mammals 166 million years ago (18), duplication of the -gene occurred; this was followed by differentiation into the two Ig classes unique to mammals, IgG and IgE, as indicated by their presence in monotremes (19,20). In IgG, the second domain of the heavy chain constant region condensed to form the hinge polypeptide (3), whereas in IgE, the domain was retained as C⑀2 so that, like IgY, the Fc fragment consists of three constant Ig domain pairs.…”

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confidence: 99%

Avian IgY Binds to a Monocyte Receptor with IgG-like Kinetics Despite an IgE-like Structure

Taylor¹,

Gould

Sutton

et al. 2008

Journal of Biological Chemistry

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An ancestor of avian IgY was the evolutionary precursor of mammalian IgG and IgE, and present day chicken IgY performs the function of human IgG despite having the domain structure of human IgE. The kinetics of IgY binding to its receptor on a chicken monocyte cell line, MQ-NCSU, were measured, the first time that the binding of a non-mammalian antibody to a nonmammalian cell has been investigated (k ؉1 ‫؍‬ 1.14 ؎ 0. 46 ). IgE has an extra pair of immunoglobulin domains when compared with IgG. Their presence reduces the dissociation rate of IgE from its receptor 20-fold, thus contributing to the high affinity of IgE. To assess the effect of the equivalent domains on the kinetics of IgY binding, IgY-Fc fragments with and without this domain were cloned and expressed in mammalian cells. In contrast to IgE, their presence in IgY has little effect on the association rate and no effect on dissociation. Whatever the function of this extra domain pair in avian IgY, it has persisted for at least 310 million years and has been co-opted in mammalian IgE to generate a uniquely slow dissociation rate and high affinity.IgY is the principal serum antibody of amphibians, reptiles, and birds and shares a common ancestor with both mammalian IgG and IgE (1, 2). The cDNA sequence of the chicken upsilon () heavy chain (3) reveals that, like more basal amphibian IgY (4, 5), avian IgY contains a domain pair (C2) 4 that has been conserved in mammalian IgE (as C⑀2) but truncated to form the "hinge" region in mammalian IgG (3). Thus, an orthologous domain pair must have existed in the common (IgY-like) ancestor prior to its duplication and subsequent divergence in the mammalian lineage. Avian IgY is the closest extant protein to this ancestor and therefore the most logical choice for study of the evolution of modern IgG and IgE from an ancient IgY-like ancestor.IgG, the principal mammalian serum antibody, aggregates and facilitates opsonization of antigens, activates complement, and provides protection for the fetus following transport across the placenta. IgE does not activate complement nor cross the placenta but can sensitize effector cells (principally mast cells and basophils) and typically mediates anaphylactic reactions (6). It is well known for its involvement in allergic disease but probably also provides defense against parasitic infections (7).Avian IgY appears to combine the functions of mammalian IgG and IgE. As the major serum antibody, it provides defense against infection (8) but also mediates anaphylaxis (9). Chicken mast cells activated by IgY are responsible for local anaphylactic reactions in the gut, which play a role in defense against protozoan infections (10, 11). Antibody-dependent hypersensitivity and fatal systemic anaphylactic shock have also been demonstrated in chickens (9, 12, 13) and shown to be mediated by basophils (14), which are much more numerous than mast cells in birds (in contrast to mammals in which the reverse is true) (15). These phenomena constitute indirect evidence for the presence of IgY...

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Vertebrate Immune System Evolution and Comparative Primate Immunity

Brinkworth

Thorn

2013

Primates, Pathogens, and Evolution

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Cloning of IgE from the echidna (Tachyglossus aculeatus) and a comparative analysis of ε chains from all three extant mammalian lineages

Cited by 54 publications

References 59 publications

Inefficient processing of mRNA for the membraneform of IgE is a genetic mechanism to limit recruitment of IgE‐secreting cells

Inefficient processing of mRNA for the membraneform of IgE is a genetic mechanism to limit recruitment of IgE‐secreting cells

Avian IgY Binds to a Monocyte Receptor with IgG-like Kinetics Despite an IgE-like Structure

Vertebrate Immune System Evolution and Comparative Primate Immunity

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