SARS-CoV accessory protein 7a directly interacts with human LFA-1
SARS-CoV accessory protein 7a directly interacts with human LFA-1
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DOI：
10.1515/bc.2007.157
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发表时间：
2007-12-01
影响因子：
3.7
通讯作者：
Willbold, Dieter
中科院分区：
文献类型：
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作者：
Haenel, Karen;Willbold, Dieter
sars冠状病毒附属蛋白7a是一种I型膜蛋白，胞外结构域有81个氨基酸残基。它被描述为在感染期间表达，并且是病毒颗粒表面的一个组成部分。在这项研究中，我们证明了蛋白7a直接特异性结合Jurkat细胞表面的人淋巴细胞功能相关抗原1 （LFA-1）。用磷酯人工激活细胞后，结合增强。通过将重组蛋白7a与野生型和突变型K287C/K294C I结构域直接体外结合，证实了这些观察结果，表明I结构域是LFA-1 U-L链上7a的结合位点。讨论了LFA-1与7a相互作用的后果。特别是，我们的数据表明LFA-1可能是SARS-CoV在人白细胞上的附着因子或受体。
The SARS-CoV accessory protein 7a is a type I membrane protein with an extracellular domain of 81 amino acid residues. It is described to be expressed during infection and to be a component of the virus particle surface. In this study, we demonstrate that protein 7a binds directly and specifically to human lymphocyte function-associated antigen 1 (LFA-1) on the cell surface of Jurkat cells. The binding is increased upon artificial cell activation with phorbol ester. These observations are confirmed by direct in vitro binding of recombinant protein 7a to the wild type and mutant K287C/K294C I domain showing that the I domain is the 7a binding site in the U-L chain of LFA-1. Consequences of the LFA-1 interaction with 7a are discussed. In particular, our data suggest LFA-1 to be an attachment factor or the receptor for SARS-CoV on human leukocytes.