Herold B C, Visalli R J, Susmarski N, Brandt C R, Spear P G
Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, Illinois 60611.
J Gen Virol. 1994 Jun;75 ( Pt 6):1211-22. doi: 10.1099/0022-1317-75-6-1211.
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, as 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.
先前的研究表明，单纯疱疹病毒（HSV）与细胞的初始相互作用是与硫酸乙酰肝素结合，且HSV-1糖蛋白C（gC）主要负责这种结合。尽管gC阴性病毒突变体在结合和进入方面存在缺陷，但它们仍保留显著的感染性。本文报道的研究目的是探索gC阴性HSV-1突变体感染性的必要条件。我们发现，细胞表面硫酸乙酰肝素的缺失或改变显著降低了gC阴性突变病毒的结合，并使细胞对感染产生抗性，这与野生型病毒的情况一致。我们分离出一种重组双突变HSV毒株，该毒株产生的病毒粒子缺乏两种已知的肝素结合糖蛋白gB和gC。相对于gC阴性和野生型病毒粒子，这些突变病毒粒子与细胞的结合能力大幅受损，这表明gB介导了gC阴性病毒粒子与细胞的结合。因此，至少两种HSV糖蛋白可以独立介导HSV与细胞表面硫酸乙酰肝素的结合，从而启动病毒进入细胞的过程。
