Possible mode of antiviral activity of acidic protein bound polysaccharideisolated from Ganoderma lucidum on herpes simplex viruses

Citation
Sk. Eo et al., Possible mode of antiviral activity of acidic protein bound polysaccharideisolated from Ganoderma lucidum on herpes simplex viruses, J ETHNOPHAR, 72(3), 2000, pp. 475-481
Citations number
22
Categorie Soggetti
Pharmacology & Toxicology
Journal title
JOURNAL OF ETHNOPHARMACOLOGY
ISSN journal
03788741 → ACNP
Volume
72
Issue
3
Year of publication
2000
Pages
475 - 481
Database
ISI
SICI code
0378-8741(200010)72:3<475:PMOAAO>2.0.ZU;2-S
Abstract
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 DE AE-cellulose column chromatography. Their antiviral activities against herp es simplex virus type 1 (HSV-1) and type 2 (HSV-2) were then investigated b y plaque reduction assay. APBP exhibited more potent HSV-1 and HSV-2 antivi ral activity than NPBP with 50% effective concentration (EC50) of 300-520 m u 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 h ave a direct virucidal effect on HSV-1 and HSV-2. APBP did not induce IFN o r 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 m u g/ml inhibited up to 500/u of the attachment of HSV-1 and HSV-2 to Vero c ells and was also found to prevent penetration of both types of HSV into Ve ro cells. These results show that the antiherpetic activity of APBP seems t o 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 Lt d. All rights reserved.