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本文引用的文献

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Linkage of superantigen-like stimulation of syngeneic T cells in a mouse model of follicular center B cell lymphoma to transcription of endogenous mammary tumor virus.在滤泡中心B细胞淋巴瘤小鼠模型中，同基因T细胞的超抗原样刺激与内源性乳腺肿瘤病毒转录的关联。
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Science. 1993 Nov 5;262(5135):909-11. doi: 10.1126/science.7694363.
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Tumor rejection after direct costimulation of CD8+ T cells by B7-transfected melanoma cells.通过B7转染的黑色素瘤细胞直接共刺激CD8 + T细胞后的肿瘤排斥反应。
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Induction of alloantigen-specific hyporesponsiveness in human T lymphocytes by blocking interaction of CD28 with its natural ligand B7/BB1.通过阻断CD28与其天然配体B7/BB1的相互作用诱导人T淋巴细胞中的同种抗原特异性低反应性。
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10
In vitro induction of T cell anergy by blocking B7 and early T cell costimulatory molecule ETC-1/B7-2.通过阻断B7和早期T细胞共刺激分子ETC-1/B7-2在体外诱导T细胞无能
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B7的突变分析及一种可变剪接产物确定了其在免疫球蛋白C样结构域上的CD28/CTLA4结合位点。

Mutational analysis and an alternatively spliced product of B7 defines its CD28/CTLA4-binding site on immunoglobulin C-like domain.

作者信息

Guo Y, Wu Y, Zhao M, Kong X P, Liu Y

机构信息

Michael Heidelberger Division of Immunology, Department of Pathology, New York University Medical Center, New York 10016, USA.

出版信息

J Exp Med. 1995 Apr 1;181(4):1345-55. doi: 10.1084/jem.181.4.1345.

DOI:10.1084/jem.181.4.1345
PMID:7535334
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2191977/
Abstract

Costimulatory molecules B7 and B7-2 interact with T cell surface receptors CD28/CTLA4 and deliver a costimulatory signal essential for T cell growth. However, the structure basis of this interaction is not known. B7 and B7-2 are members of immunoglobulin (Ig) superfamily and their extracellular portion consists of an IgV- and IgC-like domain. Here we report that a naturally occurring, alternatively spliced form of B7 reveals that exon 3-encoded IgC domain is essential for CD28/CTLA4 binding. Mutational analysis of B7 demonstrates a critical role of several amino acids around loops between strands B and C and D and E, for binding CTLA4/CD28. These amino acids are clustered to form a single binding site centered at 201Y. A comparison of the effects of mutations on the binding of CD28 and CTLA4 reveals that CD28 and CTLA4 binds to the same site on B7. These results have important implications on the role of CTLA4 and CD28 in T cell costimulation. The structure of the CD28/CTLA4-binding site also provides valuable information for immune intervention targeted at the B7/B7-2-CD28/CTLA4 interactions.

摘要

共刺激分子B7和B7-2与T细胞表面受体CD28/CTLA4相互作用，并传递T细胞生长所必需的共刺激信号。然而，这种相互作用的结构基础尚不清楚。B7和B7-2是免疫球蛋白（Ig）超家族成员，其细胞外部分由一个IgV样结构域和一个IgC样结构域组成。在此我们报道，一种天然存在的、选择性剪接形式的B7表明，外显子3编码的IgC结构域对于CD28/CTLA4结合至关重要。对B7的突变分析表明，在B链与C链以及D链与E链之间的环周围的几个氨基酸对于结合CTLA4/CD28起着关键作用。这些氨基酸聚集形成一个以201Y为中心的单一结合位点。对突变对CD28和CTLA4结合影响的比较表明，CD28和CTLA4与B7上的同一位点结合。这些结果对于CTLA4和CD28在T细胞共刺激中的作用具有重要意义。CD28/CTLA4结合位点的结构也为针对B7/B7-2-CD28/CTLA4相互作用的免疫干预提供了有价值的信息。