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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Regulation of CD45 engagement by the B-cell receptor CD22.
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Regulation of CD45 engagement by the B-cell receptor CD22.

机译：B细胞受体CD22对CD45参与的调节。

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摘要

The B-cell receptor CD22 binds sialic acid linked alpha-2-6 to terminal galactose residues on N-linked oligosaccharides associated with several cell-surface glycoproteins. The first of these sialoglycoproteins to be identified was the receptor-linked phosphotyrosine phosphatase CD45, which is required for antigen/CD3-induced T-cell activation. In the present work, we examine the effect of interaction between the extracellular domain of CD45 and CD22 on T-cell activation. Using soluble CD22-immunoglobulin fusion proteins and T cells expressing wild-type and chimeric CD45 forms, we show that engagement of CD45 by soluble CD22 can modulate early T-cell signals in antigen receptor/CD3-mediated stimulation. We also show that addition of sialic acid by beta-galactoside alpha-2,6-sialyltransferase to the CD22 molecule abrogates interactions between CD22 and its ligands. Together, these observations provide direct evidence for a functional role of the interaction between the extracellular domain of CD45 and a natural ligand and suggest another regulatory mechanism for CD22-mediated ligand engagement.
机译：B细胞受体CD22将唾液酸连接的α-2-6结合到与几种细胞表面糖蛋白相关的N连接的寡糖上的末端半乳糖残基上。首先鉴定出这些唾液糖蛋白是受体连接的磷酸酪氨酸磷酸酶CD45，这是抗原/ CD3诱导的T细胞活化所必需的。在本工作中，我们研究了CD45和CD22的胞外域之间相互作用对T细胞活化的影响。使用可溶性CD22-免疫球蛋白融合蛋白和表达野生型和嵌合CD45形式的T细胞，我们表明可溶性CD22参与CD45可以调节抗原受体/ CD3介导的刺激中的早期T细胞信号。我们还表明，通过β-半乳糖苷α-2,6-唾液酸转移酶向CD22分子添加唾液酸可消除CD22及其配体之间的相互作用。总之，这些发现为CD45的胞外域与天然配体之间相互作用的功能作用提供了直接证据，并提出了CD22介导的配体结合的另一种调节机制。

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