Isolation, identification and function of a novel anti-HSV-1 protein from Grifola frondosa
| Autor: | Jun-Wen Li, Min Jin, Zhi-Qiang Shen, Chang-Qing Gu, Fu-Huan Chao, Xin Wei Wang |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Antiviral protein
Herpesvirus 1 Human Biology Virus Replication Tandem mass spectrometry medicine.disease_cause Antiviral Agents Cell Line Cornea Fungal Proteins Mice Virology medicine Animals Grifola frondosa Ammonium sulfate precipitation Pharmacology Gel electrophoresis chemistry.chemical_classification Mice Inbred BALB C Herpes Simplex Amino acid Matrix-assisted laser desorption/ionization Herpes simplex virus chemistry Biochemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Keratitis Herpetic Female Grifola |
| Zdroj: | Antiviral Research. 75:250-257 |
| ISSN: | 0166-3542 |
| DOI: | 10.1016/j.antiviral.2007.03.011 |
| Popis: | A novel antiviral protein was purified from an extract of Grifola frondosa fruiting bodies using a procedure that included 40% ammonium sulfate precipitation and DEAE-cellulose ion exchange chromatography, and designated GFAHP. This protein inhibited herpes simplex virus type 1 (HSV-1) replication in vitro with an IC(50) value of 4.1 microg/ml and a therapeutic index >29.3. Higher concentrations of GFAHP (125 and 500 microg/ml) also significantly reduced the severity of HSV-1 induced blepharitis, neovascularization, and stromal keratitis in a murine model. Topical administration of GFAHP to the mouse cornea resulted in a significant decrease in virus production (mean virus yields: 3.4log10PFU in the treated group and 4.19log10PFU in the control group). We proved that GFAHP directly inactivates HSV-1 while simultaneously inhibiting HSV-1 penetration into Vero cells. Gel electrophoresis showed that GFAHP had a molecular weight of 29.5 kDa. GFAHP was tryptic digested and analyzed from the PMF of matrix assisted desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) and nanoelectrospray ionization tandem mass spectrometry. The N-terminal sequence of GFAHP consisted of an 11 amino acid peptide, NH(2)-REQDNAPCGLN-COOH that did not match any known amino acid sequences, indicating that GFAHP is likely to be a novel antivirus protein. To our knowledge, this is the first report that characterizes an anti-HSV protein from G. frondosa. |
| Databáze: | OpenAIRE |
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