T-cell receptors in ectothermic vertebrates

被引:39
作者
Charlemagne, J
Fellah, JS
De Guerra, A
Kerfourn, F
Partula, S
机构
[1] Univ Paris 06, Grp Immunol Comparee, F-75252 Paris 05, France
[2] CNRS, UMR 7622, F-75252 Paris 05, France
关键词
D O I
10.1111/j.1600-065X.1998.tb01255.x
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
The structure and expression of genes encoding molecules homologous to mammalian T-cell receptors (TCR) have been recently studied in ectothermic vertebrate species representative of chondrychthians, teleosts, and amphibians. The overall TCR chain structure is well conserved in phylogeny: TCR beta- and TCR alpha-like chains were detected in all the species analyzed; TCR gamma- and TCR delta-like chains were also present in a chondrychthian species. The diversity potential of the variable (V) and joining (J) segments is rather large and, as in mammals, conserved diversity (D) segments are associated to the TCR beta and TCR delta chains. An important level of junctional diversity occurred at the V-(D)-J junctions, with the potential addition of N- and P-nucleotides. Thus, the conservation of the structure and of the potential of diversity of TCR molecules have been under a permanent selective pressure during vertebrate evolution. The structure of MHC class I and class II molecules was also well conserved in jawed vertebrates. TCR and MHC molecules are strongly functionally linked and play a determinant role in the initiation and the regulation of the specific immune responses; thus, it is not surprising that their structures have been reciprocally frozen during evolution.
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页码:87 / 102
页数:16
相关论文
共 35 条
[1]  
ALCOVER A, 1990, J BIOL CHEM, V265, P4134
[2]   The interchain disulfide bond between TCR alpha beta heterodimers on human T cells is not required for TCR-CD3 membrane expression and signal transduction [J].
Arnaud, J ;
Huchenq, A ;
Vernhes, MC ;
CasparBauguil, S ;
Lenfant, F ;
Sancho, J ;
Terhorst, C ;
Rubin, B .
INTERNATIONAL IMMUNOLOGY, 1997, 9 (04) :615-626
[3]   Signaling efficiency of the T cell receptor controlled by a single amino acid in the beta chain constant region [J].
Backstrom, BT ;
Hausmann, BT ;
Palmer, E .
JOURNAL OF EXPERIMENTAL MEDICINE, 1997, 186 (11) :1933-1938
[4]   A motif within the T cell receptor alpha chain constant region connecting peptide domain controls antigen responsiveness [J].
Backstrom, BT ;
Milia, E ;
Peter, A ;
Jaureguiberry, B ;
Baldari, CT ;
Palmer, E .
IMMUNITY, 1996, 5 (05) :437-447
[5]   CRYSTAL-STRUCTURE OF THE BETA-CHAIN OF A T-CELL ANTIGEN RECEPTOR [J].
BENTLEY, GA ;
BOULOT, G ;
KARJALAINEN, K ;
MARIUZZA, RA .
SCIENCE, 1995, 267 (5206) :1984-1987
[6]  
Campbell K S, 1994, Semin Immunol, V6, P393, DOI 10.1006/smim.1994.1049
[7]  
CASPARBAUGUIL S, 1994, C R ACAD SCI 3, V313, P77
[8]  
CHARLEMAGNE J, 1997, IMMUNOLOGICAL METHOD, P2340
[9]   THE OUTLINE STRUCTURE OF THE T-CELL ALPHA-BETA-RECEPTOR [J].
CHOTHIA, C ;
BOSWELL, DR ;
LESK, AM .
EMBO JOURNAL, 1988, 7 (12) :3745-3755
[10]   The T cell receptor beta genes of Xenopus [J].
Chretien, I ;
Marcuz, A ;
Fellah, J ;
Charlemagne, J ;
DuPasquier, L .
EUROPEAN JOURNAL OF IMMUNOLOGY, 1997, 27 (03) :763-771