- 著者
- 
             
             Sangchai Yingsakmongkon
             
             Daisei Miyamoto
             
             Nongluk Sriwilaijaroen
             
             Kimie Fujita
             
             Kosai Matsumoto
             
             Wipawee Jampangern
             
             Hiroaki Hiramatsu
             
             Chao-Tan Guo
             
             Toshihiko Sawada
             
             Tadanobu Takahashi
             
             Kazuya Hidari
             
             Takashi Suzuki
             
             Morihiro Ito
             
             Yasuhiko Ito
             
             Yasuo Suzuki
             
          
- 出版者
- The Pharmaceutical Society of Japan
- 雑誌
- Biological and Pharmaceutical Bulletin (ISSN:09186158)
- 巻号頁・発行日
- vol.31, no.3, pp.511-515, 2008-03-01 (Released:2008-03-01)
- 参考文献数
- 30
- 被引用文献数
- 
             
             42
             
             
             46
             
             
          
        
        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 μg/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.