ArticleProceedings of the National Academy of Sciences of the United States of America1996
A new high molecular weight immunoglobulin class from the carcharhine shark: implications for the properties of the primordial immunoglobulin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Mass Spectrometry Analysis of Shark Skin Proteins.International journal of molecular sciences · 2023Review
- An Ancient MHC-Linked Gene Encodes a Nonrearranging Shark Antibody, UrIg, Convergent with IgG.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- Evolution of the Immunoglobulin Isotypes-Variations of Biophysical Properties among Animal Classes.Biomolecules · 2023Article
- The immunoglobulins of cartilaginous fishes.Developmental and comparative immunology · 2021Review
- Ancient Use of Ig Variable Domains Contributes Significantly to the TCRδ Repertoire.Journal of immunology (Baltimore, Md. : 1950) · 2019Article
- Molecular Origin of the Stability Difference in Four Shark IgNAR Constant Domains.Biophysical journal · 2019Article
- A cold-blooded view of adaptive immunity.Nature reviews. Immunology · 2018Review
- Immunoglobulin T from sea bass (Dicentrarchus labrax L.): molecular characterization, tissue localization and expression after nodavirus infection.BMC molecular biology · 2017Article
- Comparative transcriptomics of elasmobranchs and teleosts highlight important processes in adaptive immunity and regional endothermy.BMC genomics · 2017Article
- Fish Immunoglobulins.Biology · 2016Review
- Article
- The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Noncoordinate expression of J-chain and Blimp-1 define nurse shark plasma cell populations during ontogeny.European journal of immunology · 2013Article
- Shark IgW C region diversification through RNA processing and isotype switching.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Extensive diversification of IgH subclass-encoding genes and IgM subclass switching in crocodilians.Nature communications · 2013Article
- Expressional analysis of immunoglobulin D in cattle (Bos taurus), a large domesticated ungulate.PloS one · 2012Article
- Origin and evolution of the adaptive immune system: genetic events and selective pressures.Nature reviews. Genetics · 2010Review
- Comparative and developmental study of the immune system in Xenopus.Developmental dynamics : an official publication of the American Association of Anatomists · 2009Review
- Ancient phylogenetic beginnings of immunoglobulin hypermutation.Journal of molecular evolution · 2006Article
- IgD, like IgM, is a primordial immunoglobulin class perpetuated in most jawed vertebrates.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
All immunoglobulins and T-cell receptors throughout phylogeny share regions of highly conserved amino acid sequence. To identify possible primitive immunoglobulins and immunoglobulin-like molecules, we utilized 3' RACE (rapid amplification of cDNA ends) and a highly conserved constant region consensus amino acid sequence to isolate a new immunoglobulin class from the sandbar shark Carcharhinus plumbeus. The immunoglobulin, termed IgW, in its secreted form consists of 782 amino acids and is expressed in both the thymus and the spleen. The molecule overall most closely resembles mu chains of the skate and human and a new putative antigen binding molecule isolated from the nurse shark (NAR). The full-length IgW chain has a variable region resembling human and shark heavy-chain (VH) sequences and a novel joining segment containing the WGXGT motif characteristic of H chains. However, unlike any other H-chain-type molecule, it contains six constant (C) domains. The first C domain contains the cysteine residue characteristic of C mu1 that would allow dimerization with a light (L) chain. The fourth and sixth domains also contain comparable cysteines that would enable dimerization with other H chains or homodimerization. Comparison of the sequences of IgW V and C domains shows homology greater than that found in comparisons among VH and C mu or VL, or CL thereby suggesting that IgW may retain features of the primordial immunoglobulin in evolution.
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