Possible mode of antiviral activity of acidic protein bound polysaccharide isolated from Ganoderma lucidum on herpes simplex viruses
Possible mode of antiviral activity of acidic protein bound polysaccharide isolated from Ganoderma lucidum on herpes simplex viruses
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DOI：
10.1016/s0378-8741(00)00266-x
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发表时间：
2000-10-01
影响因子：
5.4
通讯作者：
Han, SS
中科院分区：
文献类型：
--
作者：
Eo, SK;Kim, YS;Han, SS
采用EtOH沉淀法和deae -纤维素柱层析法从灵芝的水溶性物质中分离得到中性蛋白结合多糖（NPBP）和酸性蛋白结合多糖（APBP）。然后用斑块减少法研究它们对1型单纯疱疹病毒（HSV-1）和2型单纯疱疹病毒（HSV-2）的抗病毒活性。APBP在50%有效浓度（EC50）为300 ~ 520 μ g/ml时，对HSV-1和HSV-2的抗病毒活性高于NPBP。为了探讨APBP抗病毒作用的可能模式及其抗病毒作用，我们分别用HSV-1和HSV-2进行了预孵育、附着和渗透实验。发现APBP对HSV-1和HSV-2有直接的杀病毒作用。APBP在体外没有诱导IFN或IFN样物质，也不会诱导从正常状态到抗病毒状态的变化。浓度为100和90 μ g/ml的APBP可抑制HSV-1和HSV-2在Vero细胞上高达500/u的附着，并可阻止这两种类型的HSV侵入Vero细胞。这些结果表明，APBP的抗疱疹活性似乎与其与hsv特异性糖蛋白的结合有关，该糖蛋白负责附着和穿透，并且APBP阻碍病毒与细胞膜的复杂相互作用。(C) 2000爱思唯尔科学爱尔兰有限公司版权所有。
Two protein bound polysaccharides, a neutral protein bound polysaccharide (NPBP) and an acidic protein bound polysaccharide (APBP), were isolated from water soluble substances of Ganoderma lucidum by EtOH precipitation and DEAE-cellulose column chromatography. Their antiviral activities against herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) were then investigated by plaque reduction assay. APBP exhibited more potent HSV-1 and HSV-2 antiviral activity than NPBP with 50% effective concentration (EC50) of 300-520 mu g/ml. In order to examine the possible mode of the antiviral activity of APBP its virucidal effect, antiviral activity in preincubation, attachment and penetration assay were tested with HSV-1 and HSV-2. APBP was found to have a direct virucidal effect on HSV-1 and HSV-2. APBP did not induce IFN or IFN-like materials in vitro and is not expected to induce a change from a normal state to an antiviral state. APBP in concentrations of 100 and 90 mu g/ml inhibited up to 500/u of the attachment of HSV-1 and HSV-2 to Vero cells and was also found to prevent penetration of both types of HSV into Vero cells. These results show that the antiherpetic activity of APBP seems to be related to its binding with HSV-specific glycoproteins responsible for the attachment and penetration, and APBP impedes the complex interactions of viruses with cell plasma membranes. (C) 2000 Elsevier Science Ireland Ltd. All rights reserved.