ROLE OF THE ADENOVIRUS E3-19K CONSERVED REGION IN BINDING MAJOR HISTOCOMPATIBILITY COMPLEX CLASS-I MOLECULES
ROLE OF THE ADENOVIRUS E3-19K CONSERVED REGION IN BINDING MAJOR HISTOCOMPATIBILITY COMPLEX CLASS-I MOLECULES
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DOI：
10.1128/jvi.66.8.4778-4783.1992
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发表时间：
1992-08-01
影响因子：
5.4
通讯作者：
LUPATKIN, H
中科院分区：
文献类型：
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作者：
FLOMENBERG, P;SZMULEWICZ, J;LUPATKIN, H
腺病毒早期3区糖蛋白E3-19k结合并下调感染细胞中的主要组织相容性复合体（MHC） I类分子。我们之前通过比较四种不同腺病毒血清型的蛋白序列，在E3-19k中发现了一个20个氨基酸的保守区域。研究了E3-19k c -末端和邻近的保守区域在与MHC I类分子相互作用中的作用。从克隆的35型腺病毒E3 18.5 kda开放阅读框中表达了一个功能性的i类结合糖蛋白。腺病毒35型糖蛋白的截断和单氨基酸突变是通过定点体外诱变产生的，并测试了与MHC I类分子结合的能力。大部分跨膜结构域和细胞质尾部的缺失不影响与I类分子的结合。然而，去除另外11个氨基酸消除了结合并改变了邻近保守区域的构象。在保守区域内，残基Asp-107和Met-110的单独突变严重减少或消除了结合。这些数据表明E3-19k保守区在与MHC I类分子的结合中起着至关重要的作用。
The adenovirus early region 3 glycoprotein E3-19k binds to and down regulates major histocompatibility complex (MHC) class I molecules in infected cells. We previously identified a 20-amino-acid conserved region in E3-19k by comparison of protein sequences from four different adenovirus serotypes. The roles of the E3-19k C-terminal and adjacent conserved regions in the interaction with MHC class I molecules have been examined. A functional class I-binding glycoprotein was expressed from the cloned E3 18.5-kDa open reading frame of adenovirus type 35. Truncations and single-amino-acid mutations in the adenovirus type 35 glycoprotein were created by site-directed in vitro mutagenesis and tested for the ability to associate with MHC class I molecules. Deletion of most of the transmembrane domain and cytoplasmic tail did not affect binding to class I molecules. However, removal of an additional 11 amino acids eliminated binding and changed the conformation of the adjacent conserved region. Separate mutations of residues Asp-107 and Met-110, within the conserved region, severely reduced or eliminated binding. These data indicate that the E3-19k conserved region plays a crucial role in binding to MHC class I molecules.