The immunoglobulin heavy chain locus in the reptile Anolis carolinensis

Deza, Francisco Gambón; Espinel, Christian Sánchez; Mompó, Susana Magadán

doi:10.1016/j.molimm.2009.02.019

Cited by 27 publications

(17 citation statements)

References 17 publications

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“…The IgH locus in the amphibian Xenopus tropicalis has been shown to be arranged as V H -D H -J H -C m -C d -C x -C y -C V, where the C 4 encodes the first (genetic) hinge-containing Ig class in non-mammalian vertebrates [8,9]. Recently, four IgH isotypes, IgM, IgD, IgY, and IgA, were identified in reptiles, although the IgA encoding gene shows a punctate distribution [10][11][12]. Similar to reptiles, birds express the characteristic IgM, IgA, and IgY [13,14].…”

Section: Introductionmentioning

confidence: 99%

The immunoglobulin gene loci in the teleost Gasterosteus aculeatus

Bao

Wang

Guo

et al. 2010

Fish & Shellfish Immunology

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Section: Introductionmentioning

confidence: 99%

The immunoglobulin gene loci in the teleost Gasterosteus aculeatus

Bao

Wang

Guo

et al. 2010

Fish & Shellfish Immunology

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“…Previously (Olivieri et al 2014), we showed that such a low number of TRB V genes is common among reptiles. Monotremes arose prior to marsupials and still retain reptilelike genes which are not found in other mammals (e.g., the IgD has ten domains (Gambon Deza et al 2009)). Figure 3 (bottom left) shows the phylogenetic analysis of the Monotreme TRBV sequences with the Primate consensus sequences.…”

Section: Gene From the Trav And Trbv Loci In Monotremes And Marsupialsmentioning

confidence: 99%

Evolution of V genes from the TRV loci of mammals

2015

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Information concerning the evolution of T lymphocyte receptors (TCR) can be deciphered from that part of the molecule that recognizes antigen presented by major histocompatibility complex (MHC), namely the variable (V) regions. The genes that code for these variable regions are found within the TCR loci. Here, we describe a study of the evolutionary origin of V genes that code for the α and β chains of the TCR loci of mammals. In particular, we demonstrate that most of the 35 TRAV and 25 TRBV conserved genes found in Primates are also found in other Eutheria, while in Marsupials, Monotremes, and Reptiles, these genes diversified in a different manner. We also show that in mammals, all TRAV genes are derived from five ancestral genes, while all TRBV genes originate from four such genes. In Reptiles, the five TRAV and three out of the four TRBV ancestral genes exist, as well as other V genes not found in mammals. We also studied the TRGV and TRDV loci from all mammals, and we show a relationship of the TRDV to the TRAV locus throughout evolutionary time.

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“…More recently, genomic organization studies showed that the IgH locus of the Asian lizard ( Eublepharis macularius ) contains genes that code for IgM, IgD, IgY, and IgA [38-40]. In contrast to the Asian lizard, the IgH locus of the American lizard ( Anolis carolinensis ) codes only for IgM, IgD, and IgY [38, 41]. Taking into account the fact that both mammals and birds encode the IgA isotype, the absence of this gene in certain reptiles indicates that the IgA gene was independently lost in some reptilian lineages.…”

Section: Immunoglobulin Heavy Chainsmentioning

confidence: 99%

“…The number of genes also varies extensively between different vertebrate lineages. For example, in the frog, Xenopus tropicalis , the IgH locus contains nearly eighty V H genes followed by the five D H and seven J H [17, 42], whereas the IgH locus in anole lizards ( A. carolinensis ) contains more than 70 V H , 22 D H , and nine J H genes [38]. The IgH locus of birds has an unusual organization as compared to other tetrapods [17, 33, 34, 37].…”

Section: Immunoglobulin Heavy Chainsmentioning

confidence: 99%

Evolutionary Genomics of Immunoglobulin-Encoding Loci in Vertebrates

Das

Hirano

Tako

et al. 2012

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Immunoglobulins (or antibodies) are an essential element of the jawed vertebrate adaptive immune response system. These molecules have evolved over the past 500 million years and generated highly specialized proteins that recognize an extraordinarily large number of diverse substances, collectively known as antigens. During vertebrate evolution the diversification of the immunoglobulin-encoding loci resulted in differences in the genomic organization, gene content, and ratio of functional genes and pseudogenes. The tinkering process in the immunoglobulin-encoding loci often gave rise to lineage-specific characteristics that were formed by selection to increase species adaptation and fitness. Immunoglobulin loci and their encoded antibodies have been shaped repeatedly by contrasting evolutionary forces, either to conserve the prototypic structure and mechanism of action or to generate alternative and diversified structures and modes of function. Moreover, evolution favored the development of multiple mechanisms of primary and secondary antibody diversification, which are used by different species to effectively generate an almost infinite collection of diverse antibody types. This review summarizes our current knowledge on the genomics and evolution of the immunoglobulin-encoding loci and their protein products in jawed vertebrates.

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The immunoglobulin heavy chain locus in the reptile Anolis carolinensis

Cited by 27 publications

References 17 publications

The immunoglobulin gene loci in the teleost Gasterosteus aculeatus

The immunoglobulin gene loci in the teleost Gasterosteus aculeatus

Evolution of V genes from the TRV loci of mammals

Evolutionary Genomics of Immunoglobulin-Encoding Loci in Vertebrates

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