In vitro inhibition of human influenza A virus infection by fruit-juice concentrate of Japanese plum (Prunus mume SIEB. et ZUCC)
Autor: | Hiroaki Hiramatsu, Takashi Suzuki, Wipawee Jampangern, Yasuhiko Ito, Tadanobu Takahashi, Chao-Tan Guo, Kosai Matsumoto, Nongluk Sriwilaijaroen, Kazuya I.P.J. Hidari, Yasuo Suzuki, Daisei Miyamoto, Kimie Fujita, Morihiro Ito, Sangchai Yingsakmongkon, Toshihiko Sawada |
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Rok vydání: | 2008 |
Předmět: |
Erythrocytes
Hemagglutination viruses Guinea Pigs Pharmaceutical Science Mannose Neuraminidase Viral Plaque Assay Biology Virus Cell Line Beverages chemistry.chemical_compound Dogs Sialoglycoprotein Japanese plum Animals IC50 Hemagglutination Viral Pharmacology Dose-Response Relationship Drug Plant Extracts Monosaccharides virus diseases General Medicine Fetuin Virology chemistry Influenza A virus Galactose Fruit biology.protein Prunus |
Zdroj: | Biologicalpharmaceutical bulletin. 31(3) |
ISSN: | 0918-6158 |
Popis: | Using a plaque reduction assay, treatment of human influenza A viruses with the fruit-juice concentrate of Japanese plum (Prunus mume SIEB. et ZUCC) showed strong in vitro anti-influenza activity against human influenza A viruses before viral adsorption, but not after viral adsorption, with 50% inhibitory concentration (IC50) values against A/PR/8/34 (H1N1) virus, A/Aichi/2/68 (H3N2) virus and A/Memphis/1/71 (H3N2) virus of 6.35+/-0.17, 2.84+/-1.98 and 0.53+/-0.10 microg/ml, respectively. The plum-juice concentrate exhibited hemagglutination activity toward guinea pig erythrocytes. Its hemagglutination activity was inhibited by the monosaccharide N-acetylneuraminic acid and a sialoglycoprotein (fetuin), but not by the other tested monosaccharides (mannose, galactose, glucose and N-acetylglucosamine), suggesting the presence of a lectin-like molecule(s) in the Japanese plum-juice concentrate. Our findings suggest that the fruit-juice concentrate of Japanese plum may prevent and reduce infection with human influenza A virus, possibly via inhibition of viral hemagglutinin attachment to host cell surfaces by its lectin-like activity. |
Databáze: | OpenAIRE |
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