Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
???displayArticle.abstract???
The discovery of a fourth immunoglobulin (Ig) light (L) chain isotype in sharks has revealed the origins and natural history of all vertebrate L chains. Phylogenetic comparisons have established orthology between this new shark L chain and the unique Xenopus L chain isotype sigma. More importantly, inclusion of this new L chain family in phylogenetic analyses showed that all vertebrate L chains can be categorized into four ancestral clans originating prior to the emergence of cartilaginous fish: one restricted to elasmobranchs (sigma-cart/type I), one found in all cold-blooded vertebrates (sigma/teleost type 2/elasmobranch type IV), one in all groups except bony fish (lambda/elasmobranch type II), and one in all groups except birds (kappa/elasmobranch type III/teleost type 1 and 3). All four of these primordial L chain isotypes (sigma, sigma-cart, lambda and kappa) have maintained separate V region identities since their emergence at least 450 million years ago, suggestive of an ancient physiological distinction of the L chains. We suggest that, based upon unique, discrete sizes of complementarity determining regions 1 and 2 and other features of the V region sequences, the different L chain isotypes arose to provide different functional conformations in the Ig binding site when they pair with heavy chains.
Barré,
Structural conservation of hypervariable regions in immunoglobulins evolution.
1994, Pubmed
Barré,
Structural conservation of hypervariable regions in immunoglobulins evolution.
1994,
Pubmed
Bartl,
Identification of class I genes in cartilaginous fish, the most ancient group of vertebrates displaying an adaptive immune response.
1997,
Pubmed
Bengtén,
Immunoglobulin isotypes: structure, function, and genetics.
2000,
Pubmed
Chang,
The CDR1 sequences of a major proportion of human germline Ig VH genes are inherently susceptible to amino acid replacement.
1994,
Pubmed
Dooley,
Antibody repertoire development in cartilaginous fish.
2006,
Pubmed
Dooley,
Shark immunity bites back: affinity maturation and memory response in the nurse shark, Ginglymostoma cirratum.
2005,
Pubmed
Doyle,
Consequences of receptor editing at the lambda locus: multireactivity and light chain secretion.
2006,
Pubmed
Fleurant,
Shark Ig light chain junctions are as diverse as in heavy chains.
2004,
Pubmed
Ghaffari,
Structure and genomic organization of a second class of immunoglobulin light chain genes in the channel catfish.
1997,
Pubmed
Greenberg,
Isolation of a shark immunoglobulin light chain cDNA clone encoding a protein resembling mammalian kappa light chains: implications for the evolution of light chains.
1993,
Pubmed
Greenberg,
A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks.
1995,
Pubmed
Haire,
A third Ig light chain gene isotype in Xenopus laevis consists of six distinct VL families and is related to mammalian lambda genes.
1996,
Pubmed
,
Xenbase
Hershberg,
Differences in potential for amino acid change after mutation reveals distinct strategies for kappa and lambda light-chain variation.
2006,
Pubmed
Hill,
The evolutionary origins of the immunoglobulins.
1966,
Pubmed
Hinds,
Major reorganization of immunoglobulin VH segmental elements during vertebrate evolution.
,
Pubmed
Hohman,
Complete sequence of a cDNA clone specifying sandbar shark immunoglobulin light chain: gene organization and implications for the evolution of light chains.
1992,
Pubmed
Hsu,
Diverse immunoglobulin light chain organizations in fish retain potential to revise B cell receptor specificities.
2006,
Pubmed
Hsu,
Light chain heterogeneity in the amphibian Xenopus.
1991,
Pubmed
,
Xenbase
Johansson,
High variability in complementarity-determining regions compensates for a low number of V gene families in the lambda light chain locus of the platypus.
2005,
Pubmed
Kokubu,
Diverse organization of immunoglobulin VH gene loci in a primitive vertebrate.
1988,
Pubmed
Lee,
Hypermutation in shark immunoglobulin light chain genes results in contiguous substitutions.
2002,
Pubmed
Lee,
Rearrangement of immunoglobulin genes in shark germ cells.
2000,
Pubmed
Lewis,
The old and the restless.
2000,
Pubmed
Lewis,
Novel strand exchanges in V(D)J recombination.
1988,
Pubmed
Lobb,
Immunoglobulin light chain classes in a teleost fish.
1984,
Pubmed
Miracle,
Complex expression patterns of lymphocyte-specific genes during the development of cartilaginous fish implicate unique lymphoid tissues in generating an immune repertoire.
2001,
Pubmed
Ohta,
Primitive synteny of vertebrate major histocompatibility complex class I and class II genes.
2000,
Pubmed
Padlan,
Anatomy of the antibody molecule.
1994,
Pubmed
Pilström,
The immunoglobulin light chain in poikilothermic vertebrates.
1998,
Pubmed
Rast,
Immunoglobulin light chain class multiplicity and alternative organizational forms in early vertebrate phylogeny.
1994,
Pubmed
Richards,
The evolution of vertebrate antigen receptors: a phylogenetic approach.
2000,
Pubmed
Rumfelt,
Unprecedented multiplicity of Ig transmembrane and secretory mRNA forms in the cartilaginous fish.
2004,
Pubmed
Rumfelt,
A shark antibody heavy chain encoded by a nonsomatically rearranged VDJ is preferentially expressed in early development and is convergent with mammalian IgG.
2001,
Pubmed
Rumfelt,
Diversity and repertoire of IgW and IgM VH families in the newborn nurse shark.
2004,
Pubmed
Sakano,
Sequences at the somatic recombination sites of immunoglobulin light-chain genes.
1979,
Pubmed
Schwager,
Evolution of immunoglobulin light chain genes: analysis of Xenopus IgL isotypes and their contribution to antibody diversity.
1991,
Pubmed
,
Xenbase
Shamblott,
Complete nucleotide sequence of primitive vertebrate immunoglobulin light chain genes.
1989,
Pubmed
Shen,
Heavy-chain variable regions in carcharhine sharks: development of a comprehensive model for the evolution of VH domains among the gnathanstomes.
1996,
Pubmed
Sitnikova,
Evolution of immunoglobulin kappa chain variable region genes in vertebrates.
1998,
Pubmed
Stanfield,
Antibody elbow angles are influenced by their light chain class.
2006,
Pubmed
Sverremark,
Kappa-deficient mice are non-responders to dextran B512: is this unresponsiveness due to specialization of the kappa and lambda Ig repertoires?
2000,
Pubmed
Tonegawa,
Somatic generation of antibody diversity.
1983,
Pubmed
Zezza,
Genes encoding Xenopus laevis Ig L chains. Implications for the evolution of kappa and lambda chains.
1992,
Pubmed
,
Xenbase
