Publications (4)7.23 Total impact
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Article: Purification and characterization of a novel lectin with antiphytovirus activities from the wild mushroom Paxillus involutus.
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ABSTRACT: A novel lectin was isolated from the dried fruiting bodies of the wild mushroom Paxillus involutus. Isolation was conducted by anion exchange chromatography on DEAE-Cellulose, Q-Sepharose and gel filtration on Superdex 75 using a fast protein liquid chromatography (FPLC) system. This lectin had a molecular mass of 28 kDa and was composed of four identical subunits, each with a molecular mass of 7 kDa. N-terminal amino acid sequence of the P. involutus lectin was determined to be CTCAVFLNNTTVKS, which showed a low level of similarity to mushroom lectin sequences reported previously. The biochemical properties of this lectin were determined, and the hemagglutinating activity was inhibited by inulin and O-Nitrophenyl-β-D-galacto-pyranoside. Additionally, Ca2+, Zn2+, Cd2+, Fe2+, and Al3+ inhibited its hemagglutinating activity, while Cu2+ promoted this activity. This lectin exhibited poor thermostability and was sensitive to HCl, but it had a high tolerance to NaOH exposure. In terms of biological properties, this lectin manifested antiphytovirus activity towards tobacco mosaic virus (TMV) with a 70.61% inhibition at a concentration of 200 μg/mL. This lectin was devoid of inhibitory activities toward pathogenic fungi and HIV-1 reverse transcriptase, and antiproliferative activities were observed in tumor cell lines including lung cancer A-549 and human colon cancer HCT-8 cells.Protein and Peptide Letters 10/2012; · 1.94 Impact Factor -
Article: Cordysobin, a novel alkaline serine protease with HIV-1 reverse transcriptase inhibitory activity from the medicinal mushroom Cordyceps sobolifera.
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ABSTRACT: A novel serine protease, designated as cordysobin, was purified from dried fruiting bodies of the mushroom Cordyceps sobolifera. The isolation procedure utilized ion exchange chromatography on DEAE-cellulose and SP-Sepharose followed by gel filtration on Superdex 75. The protease did not adsorb on DEAE-cellulose but bound to SP-Sepharose. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the protease resolved as a single band with an apparent molecular mass of 31 kDa. Its optimal pH was 10.0, and the optimal temperature was 65°C. The protease displayed a K(m) value of 0.41 μM and 13.44 μM·min⁻¹ using Suc-Leu-Leu-Val-Tyr-MCA as substrate at pH 10.0 and 37°C. Protease activity was enhanced by the Fe²⁺ ion at low concentration range of 1.25-10 mM and was strongly inhibited by Hg²⁺ up to 1.25 mM. The protease was strongly inhibited by chymostatin and phenylmethylsulfonyl fluoride (PMSF), suggesting that it is a serine protease. It manifested significant inhibitory activity toward HIV-1 reverse transcriptase (RT) with an IC₅₀ value of 8.2×10⁻³ μM, which is the highest anti-HIV-1 RT activity of reported mushroom proteins.Journal of Bioscience and Bioengineering 01/2012; 113(1):42-7. · 1.79 Impact Factor -
Article: An antiproliferative ribonuclease from fruiting bodies of the wild mushroom Russula delica.
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ABSTRACT: An antiproliferative ribonuclease with a new N-terminal sequence was purified from fruiting bodies of the edible wild mushroom Russula delica in this study. This novel ribonuclease was unadsorbed on DEAE-cellulose, but absorbed on SP-Sepharose and Q-Sepharose. It had a molecular mass of 14 kDa as judged by fast protein liquid chromatography on Superdex 75 and SDS-polyacrylamide gel electrophoresis. Its optimal pH and optimal temperature were pH 5 and 60 degrees , respectively. The ranking of its activity toward various polyhomoribonucleotides was poly C > poly G > poly A > poly U. It could inhibit proliferation of HepG2 and MCF-7 cancer cells with an IC50 value of 8.6 microM and 7.2 microM, respectively. It was devoid of antifungal and HIV-1 reverse transcriptase inhibitory activity.Journal of Microbiology and Biotechnology 04/2010; 20(4):693-9. · 1.38 Impact Factor -
Article: A novel lectin with highly potent antiproliferative and HIV-1 reverse transcriptase inhibitory activities from the edible wild mushroom Russula delica.
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ABSTRACT: A dimeric lectin with a molecular weight of 60 kDa and high hemagglutinating activity was isolated from fresh fruiting bodies of the wild mushroom Russula delica. The lectin was composed of two identical subunits, each with a molecular weight of 30 kDa. It was adsorbed on both SP-Sepharose and Q-Sepharose and unadsorbed on DEAE-cellulose. Its hemagglutinating activity was stable up to 70 degrees C, and in HCl and NaOH solutions of concentrations up to 25 and 12.5 mM, respectively. The activity was inhibited by inulin and o-nitrophenyl-beta-D-galactopyranoside. Al3+, Fe3+ and Zn2+ ions, but not by Ca2+, Mg2+ and Mn2+ ions. Mg2+ ions at 10 mM concentration potentiated the hemagglutinating activity of the lectin. Russula delica lectin was devoid of mitogenic activity toward mouse splenocytes, but potently inhibited proliferation of HepG2 hepatoma and MCF 7 breast cancer cells, with an IC50 value of 0.88 microM and 0.52 microM, respectively. It potently inhibited HIV-1 reverse transcriptase activity with an IC50 of 0.26 microM.Glycoconjugate Journal 02/2010; 27(2):259-65. · 2.12 Impact Factor
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Institutions
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2010
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China Agricultural University
- State Key Laboratory for Agrobiotechnology
Beijing, Beijing Shi, China
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