Genetic organization of the human T-cell receptor γ and δ loci

Lefranc, Marie‐Paule; Rabbitts, Terence H.

doi:10.1016/0923-2494(90)90058-7

Cited by 30 publications

(13 citation statements)

References 52 publications

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“…The TRD locus is composed of a cluster of one TRDV gene (TRDV2), three TRDD genes, and four TRDJ genes, upstream of the unique TRDC gene (Lefranc, 2001). Another TRDV gene (TRDV3) is located downstream of the TRDC gene, in inverted transcription orientation (Lefranc and Rabbitts, 1990). Resembling the five TRAV/DV gene segments, TRDV1 is dispersed in the TRAV cluster rather than TRDV2 and TRDV3 (Lefranc, 2001).…”

Section: Resultsmentioning

confidence: 99%

Characterization of human αβTCR repertoire and discovery of D-D fusion in TCRβ chains

Liu

Yang

et al. 2014

Protein Cell

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The characterization of the human T-cell receptor (TCR) repertoire has made remarkable progress, with most of the work focusing on the TCRβ chains. Here, we analyzed the diversity and complexity of both the TCRα and TCRβ repertoires of three healthy donors. We found that the diversity of the TCRα repertoire is higher than that of the TCRβ repertoire, whereas the usages of the V and J genes tended to be preferential with similar TRAV and TRAJ patterns in all three donors. The V-J pairings, like the V and J gene usages, were slightly preferential. We also found that the TRDV1 gene rearranges with the majority of TRAJ genes, suggesting that TRDV1 is a shared TRAV/DV gene (TRAV42/DV1). Moreover, we uncovered the presence of tandem TRBD (TRB D gene) usage in ~2% of the productive human TCRβ CDR3 sequences.Electronic supplementary materialThe online version of this article (doi:10.1007/s13238-014-0060-1) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Characterization of human αβTCR repertoire and discovery of D-D fusion in TCRβ chains

Liu

Yang

et al. 2014

Protein Cell

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“…Both ␣␤TCR and ␥␦TCR are derived from the random rearrangement of a limited set of variable (V), diversity (D), and junctional (J) or of V and J gene segments in the TCR gene loci, respectively (1). Interestingly, the human V␦ gene locus is embedded within the V␣ gene locus, and some human V␦ genes (V␦4 to V␦8) can also be referred to as V␣ genes (V␣6, V␣21, V␣17, V␣28, and V␣14.1) (7). Because these genes can be used by both ␣␤ and ␥␦ T cells, they are termed V␣ genes when rearranged with J␣-C␣, whereas they are termed as V␦ genes when rearranged with D␦-J␦-C␦ (7).…”

mentioning

confidence: 99%

Conserved Vδ1 Binding Geometry in a Setting of Locus-Disparate pHLA Recognition by δ/αβ T Cell Receptors (TCRs): Insight into Recognition of HIV Peptides by TCRs

Shi

Kawana-Tachikawa

Gao

et al. 2017

J Virol

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Given the limited set of T cell receptor (TCR) V genes that are used to create TCRs that are reactive to different ligands, such as major histocompatibility complex (MHC) class I, MHC class II, and MHC-like proteins (for example, MIC molecules and CD1 molecules), the V␦1 segment can be rearranged with D␦-J␦-C␦ or J␣-C␣ segments to form classical ␥␦TCRs or uncommon ␣␤TCRs using a V␦1 segment (␦/␣␤TCR). Here we have determined two complex structures of the ␦/␣␤TCRs (S19-2 and TU55) bound to different locus-disparate MHC class I molecules with HIV peptides (HLA-A*2402-Nef138-10 and HLA-B*3501-Pol448-9). The overall binding modes resemble those of classical ␣␤TCRs but display a strong tilt binding geometry of the V␦1 domain toward the HLA ␣1 helix, due to a conserved extensive interaction between the CDR1␦ loop and the N-terminal region of the ␣1 helix (mainly in position 62). The aromatic amino acids of the CDR1␦ loop exploit different conformations ("aromatic ladder" or "aromatic hairpin") to accommodate distinct MHC helical scaffolds. This tolerance helps to explain how a particular TCR V region can similarly dock onto multiple MHC molecules and thus may potentially explain the nature of TCR cross-reactivity. In addition, the length of the CDR3␦ loop could affect the extent of tilt binding of the V␦1 domain, and adaptively, the pairing V␤ domains adjust their mass centers to generate differential MHC contacts, hence probably ensuring TCR specificity for a certain peptide-MHC class I (pMHC-I). Our data have provided further structural insights into the TCR recognition of classical pMHC-I molecules, unifying cross-reactivity and specificity.IMPORTANCE The specificity of ␣␤ T cell recognition is determined by the CDR loops of the ␣␤TCR, and the general mode of binding of ␣␤TCRs to pMHC has been established over the last decade. Due to the intrinsic genomic structure of the TCR ␣/␦ chain locus, some V␦ segments can rearrange with the C␣ segment, forming a hybrid V␦C␣V␤C␤ TCR, the ␦/␣␤TCR. However, the basis for the molecular recognition of such TCRs of their ligands is elusive. Here an ␣␤TCR using the V␦1 segment, S19-2, was isolated from an HIV-infected patient in an HLA-A*24:02-restricted man-

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“…The structure of the TCR ␥ gene and illustration of multiplex PCR amplification of the TCR ␥ gene are shown in Figure 1 [ Lefranc and Rabbitts, 1990]. The TCR ␥ gene includes V, J, and C gene segments with multiple subgroups within each segment.…”

Section: Multiplex Pcr Amplification Of the Tcr ␥ Genementioning

confidence: 99%

Multiplex polymerase chain reaction-based analysis of T-cell receptor ? gene rearrangements for the determination of T-lymphocyte clonality

Smith

Hsie

et al. 2000

Environ. Mol. Mutagen.

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Genetic organization of the human T-cell receptor γ and δ loci

Cited by 30 publications

References 52 publications

Characterization of human αβTCR repertoire and discovery of D-D fusion in TCRβ chains

Characterization of human αβTCR repertoire and discovery of D-D fusion in TCRβ chains

Conserved Vδ1 Binding Geometry in a Setting of Locus-Disparate pHLA Recognition by δ/αβ T Cell Receptors (TCRs): Insight into Recognition of HIV Peptides by TCRs

Multiplex polymerase chain reaction-based analysis of T-cell receptor ? gene rearrangements for the determination of T-lymphocyte clonality

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