Herpes simplex virus type 1 glycoprotein H binds to αvβ3 integrins
Herpes simplex virus type 1 glycoprotein H binds to αvβ3 integrins
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DOI：
10.1099/vir.0.80567-0
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发表时间：
2005-01-01
影响因子：
3.8
通讯作者：
Browne, H
中科院分区：
文献类型：
--
作者：
Parry, C;Bell, S;Browne, H
糖蛋白H（gH）同源物存在于疱疹病毒家族的所有成员中，gH是病毒粒子包膜糖蛋白之一，对病毒进入细胞至关重要。在这项研究中，产生了一种单纯疱疹病毒1型（HSV - 1）gH的重组可溶性形式，其中胞外域与IgG的Fc结合区融合。它与gL一起在哺乳动物细胞中表达，并且使用蛋白A琼脂糖纯化所得的gHFc - gL异二聚体。低亲和力细胞结合试验表明，gHFc - gL特异性结合于非洲绿猴肾细胞（Vero细胞），并且gH中一个潜在的整合素结合基序精氨酸 - 甘氨酸 - 天冬氨酸（RGD）的突变消除了结合。中国仓鼠卵巢细胞（CHO细胞）在该试验中未能结合。然而，表达人αvβ3整合素的CHO细胞能有效地与gHFc - gL结合，这表明HSV - 1 gH可以利用αvβ3整合素结合细胞，并且这种结合是由gH胞外域中的RGD基序介导的。
Glycoprotein H (gH) homologues are found in all members of the herpes virus family, and gH is one of the virion envelope glycoproteins that is essential for virus entry. In this study, a recombinant soluble form of Herpes simplex virus type 1 (HSV-1) gH, in which the ectodomain is fused to the Fc-binding region of IgG, has been generated. This was expressed in mammalian cells together with gL and the resulting gHFc-gL heterodimer was purified using Protein A Sepharose. Low-affinity cell binding assays showed that gHFc-gL bound specifically to Vero cells and mutation of a potential integrin-binding motif, Arg-Gly-Asp (RGD), in gH abolished binding. CHO cells failed to bind in this assay. However, CHO cells expressing the human alphavbeta3 integrin bound efficiently to gHFc-gL, suggesting that HSV-1 gH can bind to cells using alphavbeta3 integrins and that this binding is mediated by the RGD motif in the gH ectodomain.