Review: Rhinoviruses and their ICAM receptors
Review: Rhinoviruses and their ICAM receptors
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DOI：
10.1006/jsbi.1999.4143
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发表时间：
1999-12-01
影响因子：
3
通讯作者：
Rossmann, MG
中科院分区：
文献类型：
--
作者：
Bella, J;Rossmann, MG
人细胞间粘附分子-1 (ICAM-1) 的正常功能是在损伤或应激后提供内皮细胞和白细胞之间的粘附。 ICAM-1 与白细胞功能相关抗原或巨噬细胞-1 抗原结合。然而，ICAM-1 也被大多数人类鼻病毒用作受体，并且是随后病毒进入细胞期间脱壳的催化剂。 ICAM-1 的两个氨基末端结构域（D1 和 D2）的三维原子结构已确定为 2.2 埃分辨率，并适合鼻病毒-ICAM-1 复合物的冷冻电子显微镜重建。鼻病毒附着仅限于细胞膜远端氨基末端 Ig 样结构域 (D1) 的 BC、CD、DE 和 FG 环。这些环的结构与人类 ICAM-2 或鼠 ICAM-1 的结构有很大不同，后者不结合鼻病毒。 ICAM-1 和人鼻病毒之间存在广泛的电荷相互作用，这些相互作用在鼻病毒的主要和次要受体组中大多是保守的。 (C) 1999 年学术出版社。
The normal function of human intercellular adhesion molecule-1 (ICAM-1) is to provide adhesion between endothelial cells and leukocytes after injury or stress. ICAM-1 binds to leukocyte function-associated antigen or macrophage-l antigen. However, ICAM-1 is also used as a receptor by the major group of human rhinoviruses and is a catalyst for the subsequent viral uncoating during cell entry. The three-dimensional atomic structure of the two amino-terminal domains (D1 and D2) of ICAM-1 has been determined to 2.2 Angstrom resolution and fitted into a cryoelectron microscopy reconstruction of a rhino-virus-ICAM-1 complex. Rhinovirus attachment is confined to the BC, CD, DE, and FG loops of the amino-terminal Ig-like domain (D1) at the end distal to the cellular membrane. The loops are considerably different in structure to those of human ICAM-2 or murine ICAM-1, which do not bind rhinoviruses. There are extensive charge interactions between ICAM-1 and human rhinoviruses, which are mostly conserved in both major and minor receptor groups of rhinoviruses. (C) 1999 Academic Press.