THE CYTOMEGALOVIRUS US28 PROTEIN BINDS MULTIPLE CC-CHEMOKINES WITH HIGH-AFFINITY
THE CYTOMEGALOVIRUS US28 PROTEIN BINDS MULTIPLE CC-CHEMOKINES WITH HIGH-AFFINITY
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DOI：
10.1006/bbrc.1995.1814
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发表时间：
1995-06-06
影响因子：
3.1
通讯作者：
KOLATTUKUDY, PE
中科院分区：
文献类型：
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作者：
KUHN, DE;BEALL, CJ;KOLATTUKUDY, PE
人巨细胞病毒编码的几种蛋白与7种跨膜区受体高度相似。我们研究了这些蛋白质中的一种，即US28开放阅读框架的产物，与各种化学吸引配体结合的能力。US28产物与标记的趋化因子单核细胞趋化蛋白-1(MCP-1)(K-d=6.0×10(-10)M)和RANTES(K-d=2.7×10(-10)M)有较高的亲和力。这些标记的配体可以被未标记的巨噬细胞炎症蛋白MIP-1α和MIP-1β竞争结合，K-d值在1.2×10(-9)到7.5×10(-9)M之间。比较US28和其他结合趋化因子的受体的序列有助于确定负责受体-配体相互作用的区域。(C)1995年学术出版社。
Human cytomegalovirus encodes several proteins with high similarity to seven transmembrane domain receptors. We investigated the ability of one of these proteins, the product of the US28 open reading frame, to bind various chemoattractant ligands. When transfected into COS-7 cells, the US28 product conferred high affinity binding to the labeled chemokines monocyte chemoattractant protein-1 (MCP-1) (K-d = 6.0 x 10(-10) M) and RANTES (K-d = 2.7 x 10(-10) M). Binding of these labeled ligands could be competed by the unlabeled macrophage inflammatory proteins MIP-1 alpha and MIP-1 beta, with K-d values in the range 1.2 x 10(-9) to 7.5 x 10(-9) M. Comparisons of the sequences of US28 and other receptors that bind chemokines should help to define regions responsible for receptor-ligand interactions. (C) 1995 Academic Press, Inc.