MAJOR HISTOCOMPATIBILITY COMPLEX INDEPENDENT T-CELL RECEPTOR-ANTIGEN INTERACTION - FUNCTIONAL-ANALYSIS USING FLUORESCEIN DERIVATIVES

被引:25
作者
DIAMOND, DJ
SZALAY, P
SYMER, D
HAO, P
SHIN, HS
DINTZIS, RZ
DINTZIS, HM
REINHERZ, EL
SILICIANO, RF
机构
[1] JOHNS HOPKINS UNIV,SCH MED,DEPT BIOPHYS & BIOPHYS CHEM,BALTIMORE,MD 21205
[2] JOHNS HOPKINS UNIV,SCH MED,DEPT MOLEC BIOL & GENET,BALTIMORE,MD 21205
[3] JOHNS HOPKINS UNIV,SCH MED,DEPT CELL BIOL & ANAT,BALTIMORE,MD 21205
[4] JOHNS HOPKINS UNIV,SCH MED,DEPT MED,BALTIMORE,MD 21205
[5] HARVARD UNIV,SCH MED,DANA FARBER CANC INST,IMMUNOBIOL LAB,BOSTON,MA 02115
[6] HARVARD UNIV,SCH MED,DEPT MED,BOSTON,MA 02115
关键词
D O I
10.1084/jem.174.1.229
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
We have isolated T cell receptor (TCR) cDNAs from fluorescein (FL)-specific human T cell clones (alpha-FL-beta-FL), and transferred them to TCR-beta- Jurkat cells in order to study direct FL-binding to the TCR. Using either FL-conjugated polymers (FL-polymer) or FL-substituted Sepharose beads, we are able to demonstrate the direct binding of antigen to the T cell surface, and the functional activation of the T cell transfectants. We present evidence against the involvement of major histocompatibility complex (MHC) molecules or antigen presentation in the interaction of FL with the alpha-FL-beta-FL transfectants. Additionally, we have examined the effect of ring substitutions on the FL molecule as well as specific alterations of substituents attached to the 5' position, and we have found that all of them interfere with the functional recognition of the alpha-FL-beta-FL TCR. These experiments demonstrate that TCRs like antibodies have intrinsic affinities for antigen, even without the involvement of MHC molecules.
引用
收藏
页码:229 / 241
页数:13
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