An immunoglobulin heavy chain variable region gene is generated from three segments of DNA: VH, D and JH

Early, P.; Huang, Henry V.; Davis, Mark M.; Calame, Kathryn; Hood, L

doi:10.1016/0092-8674(80)90089-6

Cited by 839 publications

(399 citation statements)

References 21 publications

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“…Once considered a model epitope, PC was an intensively researched topic that helped to lay the foundation of modern immunology (27)(28)(29). Although the study of PC went out of fashion during the late 1980s, in recent years, the field has undergone a renaissance.…”

Section: Discussionmentioning

confidence: 99%

Naturally Occurring Human Phosphorylcholine Antibodies Are Predominantly Products of Affinity-Matured B Cells in the Adult

Fiskesund

Stéen

Amara

et al. 2014

The Journal of Immunology

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Phosphorylcholine (PC) is a classic T-independent Ag that is exposed on apoptotic cells, oxidized phospholipids, and bacterial polysaccharides. Experimental as well as epidemiological studies have over the past decade implicated Abs against PC (anti-PC) as anti-inflammatory and a strong protective factor in cardiovascular disease. Although clinically important, little is known about the development of anti-PC in humans. This study was conceived to dissect the human anti-PC repertoire and generate human mAbs. We designed a PC-specific probe to identify, isolate, and characterize PC-reactive B cells from 10 healthy individuals. The donors had all mounted somatically mutated Abs toward PC using a broad variety of Ig genes. PC-reactive B cells were primarily found in the IgM+ memory subset, although significant numbers also were detected among naive, IgG+, and CD27+CD43+ B cells. Abs from these subsets were clonally related, suggesting a common origin. mAbs derived from the same donors exhibited equivalent or higher affinity for PC than the well-characterized murine T-15 clone. These results provide novel insights into the cellular and molecular ontogeny of atheroprotective PC Abs, thereby offering new opportunities for Ab-based therapeutic interventions.

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Section: Discussionmentioning

confidence: 99%

Naturally Occurring Human Phosphorylcholine Antibodies Are Predominantly Products of Affinity-Matured B Cells in the Adult

Fiskesund

Stéen

Amara

et al. 2014

The Journal of Immunology

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“…There are further conserved features in the joining region, including the sequence Phe-Gly-X-Gly at amino acids 6-9. Recognition sequences for V-D and D-J recombination follow rules first established for immunoglobulin (Early et al, 1980). The recognition sequences in the T-cell receptor (-chain locus include a highly conserved heptamer with the bases TGTG situated immediately 5' to every joining region gene in both human (Siu et al, 1984a) and mouse Malissen et al, 1984).…”

Section: Discussionmentioning

confidence: 99%

Transcripts from an aberrantly re-arranged human T-cell receptor beta-chain gene.

Collins¹,

Kissonerghis²,

Dunne³

et al. 1985

The EMBO Journal

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A number of cDNA clones homologous to the human T-celi receptor ,3-chain gene have been isolated from a library constructed from the human leukaemic cell line Jurkat. The nucleotide sequences of two of these clones demonstrate thatJurkat synthesises an RNA, probably derived from an aberrantly rearranged CO1 gene, which cannot encode a fnctional /-chain. This transcript contains a novel joining region and similar transcripts appear to be relatively abundant in several T-celi lines.

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“…For the formation of a V domain, one copy of each of the three kinds of genes comes together by a special process of genetic recombination. The rearrangement involves recombination signal sequences (RSS) composed of conserved heptamers and less conserved nonamers, separated by 23-bp spacer sequence (Early et al 1980;Tonegawa 1983). The V domain can further be subdivided into the framework regions (FR) and hypervariable or complementarity-determining regions (CDR) distinguished by the extent of sequence divergence and structural delimitations.…”

Section: Introductionmentioning

confidence: 99%

Evolutionary dynamics of the immunoglobulin heavy chain variable region genes in vertebrates

et al. 2008

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Immunoglobulin heavy chains are polypeptides encoded by four genes: variable (IGHV), joining (IGHJ), diversity (IGHD), and constant (IGHC) region genes. The number of IGHV genes varies from species to species. To understand the evolution of the IGHV multigene family, we identified and analyzed the IGHV sequences from 16 vertebrate species. The results show that the numbers of functional and nonfunctional IGHV genes among different species are positively correlated. The number of IGHV genes is relatively stable in teleosts, but the intragenomic sequence variation is generally higher in teleosts than in tetrapods. The IGHV genes in tetrapods can be classified into three phylogenetic clans (I, II, and III). The clan III and/or II genes are relatively abundant, whereas clan I genes exist in small numbers or are absent in most species. The genomic organization of clan I, II, and III IGHV genes varies considerably among species, but the entire IGHV locus seems to be conserved in the subtelomeric or near-centromeric region of chromosome. The presence or absence of specific IGHV clan members and the lineage-specific expansion and contraction of IGHV genes indicate that the IGHV locus continues to evolve in a species-specific manner. Our results suggest that the evolution of IGHV multigene family is more complex than previously thought and that several factors may act synergistically for the development of antibody repertoire.

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An immunoglobulin heavy chain variable region gene is generated from three segments of DNA: VH, D and JH

Cited by 839 publications

References 21 publications

Naturally Occurring Human Phosphorylcholine Antibodies Are Predominantly Products of Affinity-Matured B Cells in the Adult

Naturally Occurring Human Phosphorylcholine Antibodies Are Predominantly Products of Affinity-Matured B Cells in the Adult

Transcripts from an aberrantly re-arranged human T-cell receptor beta-chain gene.

Evolutionary dynamics of the immunoglobulin heavy chain variable region genes in vertebrates

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