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International Immunology, Vol. 11, No. 7, 1005-1015, July 1999
© 1999 Japanese Society for Immunology

Molecular mechanisms in the TCR (TCR{alpha}ß–CD3{delta}{epsilon},{gamma}{epsilon}) interaction with {zeta}2 homodimers: clues from a `phenotypic revertant' clone

Eric P. G. Martin, Jacques Arnaud, Laeticia Alibaud, Cécile Gouaillard, Régine Llobera, Anne Huchenq-Champagne and Bent Rubin

Unité de Physiopathologie Cellulaire et Moléculaire, CNRS, ERS 1590, IFR 30 d'Immunologie Cellulaire et Moléculaire, CHU de Purpan, 31059 cedex 03 Toulouse, France

Correspondence to: B. Rubin

The association between the TCR{alpha}ß–CD3{gamma}{epsilon}{delta}{epsilon} hexamers and {zeta}2 homodimers in the endoplasmic reticulum (ER) constitutes a key step in TCR assembly and export to the T cell surface. Incompletely assembled TCR–CD3 complexes are degraded in the ER or the lysosomes. A previously described Jurkat variant (J79) has a mutation at position 195 on the TCR C{alpha} domain causing a phenylalanine to valine exchange. This results in a lack of association between TCR{alpha}ß–CD3{gamma}{epsilon}{delta}{epsilon} hexamers and {zeta}2 homodimers. Two main hypotheses could explain this phenomenon in J79 cells: TCR–CD3 hexamers may be incapable of interacting with {zeta}2 due to a structural change in the TCR C{alpha} region; alternatively, TCR–CD3 hexamers may be incapable of interacting with {zeta}2 due to factors unrelated to either molecular complex. In order to assess these two possibilities, the TCR–CD3 membrane-negative J79 cells were treated with ethylmethylsulfonate and clones positive for TCR membrane expression were isolated. The characterization of the J79r58 phenotypic revertant cell line is the subject of this study. The main question was to assess the reason for the TCR re-expression. The TCR on J79r58 cells appears qualitatively and functionally equivalent to wild-type TCR complexes. Nucleotide sequence analysis confirmed the presence of the original mutation in the TCR C{alpha} region but failed to detect compensatory mutations in {alpha}, ß, {gamma}, {delta}, {epsilon} or {zeta} chains. Thus, mutated J79-TCR–CD3 complexes can interact with {zeta}2 homodimers. Possible mechanisms for the unsuccessful TCR–CD3 interaction with {zeta}2 homodimers are presented and discussed.

Keywords: endoplasmic reticulum, Jurkat cell, molecular chaperones, point mutation, TCR

Transmitting editor: M. Reth


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