Wright J F, Kurosky A, Wasi S
Research Department, Canadian Red Cross Society, Ottawa, Ontario.
Biochem Biophys Res Commun. 1994 Feb 15;198(3):983-9. doi: 10.1006/bbrc.1994.1140.
Human cytomegalovirus was shown to bind to human umbilical vein endothelial cells in a specific, saturable and calcium-dependent manner (Kd = 7.9 pM (4 degrees C), 6469 virus binding sites/cell). Affinity adsorption of detergent-prepared lysates of surface-radiolabeled endothelial cells to virions resulted in the identification of cell-derived proteins of approximate M(r) 36,000 and 32,000 that bound cytomegalovirus. Protein sequencing of peptides obtained by cyanogen bromide cleavage demonstrated that the 36 kDa protein corresponded to human annexin II, and the 32 kDa protein was likely a degradation product. Purified annexin II was demonstrated to bind directly to virions (Kd = 57 nM, 688 annexin II binding sites/virion). These results provide evidence that an endothelial cell-surface form of annexin II acts as a receptor for cytomegalovirus, and indicate a previously undescribed role for annexin II.
人巨细胞病毒被证明以一种特异性、可饱和且依赖钙的方式与人脐静脉内皮细胞结合（解离常数Kd = 7.9皮摩尔（4摄氏度），每个细胞有6469个病毒结合位点）。用去污剂制备的表面放射性标记的内皮细胞裂解物与病毒粒子进行亲和吸附，结果鉴定出与巨细胞病毒结合的分子量约为36000和32000的细胞衍生蛋白。对溴化氰裂解得到的肽段进行蛋白质测序表明，36 kDa的蛋白对应于人膜联蛋白II，32 kDa的蛋白可能是一种降解产物。纯化的膜联蛋白II被证明可直接与病毒粒子结合（Kd = 57纳摩尔，每个病毒粒子有688个膜联蛋白II结合位点）。这些结果提供了证据，表明内皮细胞表面形式的膜联蛋白II作为巨细胞病毒的受体，并揭示了膜联蛋白II以前未被描述的作用。
