GLYCOPROTEIN-C-INDEPENDENT BINDING OF HERPES-SIMPLEX VIRUS TO CELLS REQUIRES CELL-SURFACE HEPARAN-SULFATE AND GLYCOPROTEIN-B
GLYCOPROTEIN-C-INDEPENDENT BINDING OF HERPES-SIMPLEX VIRUS TO CELLS REQUIRES CELL-SURFACE HEPARAN-SULFATE AND GLYCOPROTEIN-B
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DOI：
10.1099/0022-1317-75-6-1211
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发表时间：
1994-06-01
影响因子：
3.8
通讯作者：
SPEAR, PG
中科院分区：
文献类型：
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作者：
HEROLD, BC;VISALLI, RJ;SPEAR, PG
以前的研究表明，单纯疱疹病毒（HSV）与细胞的最初相互作用是与硫酸乙酰肝素结合，HSV-1糖蛋白C（gC）主要负责这种结合。尽管gC阴性病毒突变体的结合和进入受损，但它们保留了显著的感染性。本文报告的研究目的是探索gC阴性HSV-1突变体的感染性要求。我们发现，细胞表面硫酸乙酰肝素的缺乏或改变显着降低了GC-阴性突变病毒的结合，并使细胞对感染具有抵抗力，以前显示的野生型病毒。我们分离出一种重组的双突变HSV株，该株产生的病毒粒子不含已知的肝素结合糖蛋白gB和gC。相对于gC阴性和野生型病毒体，这些突变病毒体与细胞的结合显著受损，表明gB介导gC阴性病毒体与细胞的结合。因此，至少两种HSV糖蛋白可以独立地介导HSV与细胞表面硫酸乙酰肝素的结合，以启动病毒进入细胞的过程。
Previous studies have shown that the initial interaction of herpes simplex virus (HSV) with cells is binding to heparan sulphate and that HSV-1 glycoprotein C (gC) is principally responsible for this binding. Although gC-negative viral mutants are impaired for binding and entry, they retain significant infectivity. The purpose of the studies reported here was to explore the requirements for infectivity of gC-negative HSV-1 mutants. We found that absence or alteration of cell surface heparan sulphate significantly reduced the binding of gC-negative mutant virus and rendered cells resistant to infection, shown previously for the wild-type virus. We isolated a recombinant double-mutated HSV strain that produces virions devoid of both of the known heparin-binding glycoproteins, gB and gC. The drastically impaired binding of these mutant virions to cells, relative to gC-negative and wild-type virions, indicates that gB mediates the binding of gC-negative virions to cells. Thus at least two HSV glycoproteins can independently mediate the binding of HSV to cell surface heparan sulphate to start the process of viral entry into cells.