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Journal of Biochemistry 2006 139(3):607-614; doi:10.1093/jb/mvj067
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© 2006 The Japanese Biochemical Society.

Regular Paper

Identification and Characterization of Carbohydrate Molecules in Mammalian Cells Recognized by Dengue Virus Type 2

Chie Aoki1,*, Kazuya I.P.J. Hidari1,*, Saki Itonori2, Akihiro Yamada3, Naonori Takahashi1, Takeshi Kasama4, Futoshi Hasebe5, Mohammend Alimul Islam5, Ken Hatano3, Koji Matsuoka3, Takao Taki6, Chao-Tan Guo1,7, Tadanobu Takahashi1, Yuichi Sakano1, Takashi Suzuki1, Daisei Miyamoto1, Mutsumi Sugita2, Daiyo Terunuma3, Koichi Morita5 and Yasuo Suzuki1,{dagger}

1 Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Sciences, Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation, and COE Program in the 21st century; 2 Department of Chemistry, Faculty of Liberal Arts & Education, Shiga University; 3 Department of Functional Materials Science, Saitama University; 4 Instrumental Analysis Research Center for Life Science, Tokyo Medical and Dental University; 5 Department of Virology, Institute of Tropical Medicine, Nagasaki University, and Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation; 6 Otsuka Pharmaceutical Co., Ltd., Tokushima; and 7 Zhejiang Academy of Medical Sciences, Hang Zhou, China

{dagger} To whom correspondence should be addressed. Tel: +81-54-264-5725, Fax: +81-54-264-5721, E-mail: suzukiy{at}u-shizuoka-ken.ac.jp

The interaction between cell surface receptors and the envelope glycoprotein (EGP) on the viral membrane surface is the initial step of Dengue virus infection. To understand the host range, tissue tropism, and virulence of this pathogen, it is critical to elucidate the molecular mechanisms of the interaction of EGP with receptor molecules. Here, using a TLC/virus-binding assay, we isolated and characterized a carbohydrate molecule on mammalian cell surfaces that is recognized by dengue virus type 2 (DEN2). Structural determination by immunochemical methods showed that the carbohydrate structure of the purified glycosphingolipid was neolactotetraosylceramide (nLc4Cer). This glycosphingolipid was expressed on the cell surface of susceptible cells, such as human erythroleukemia K562 and baby hamster kidney BHK-21. All serotypes of DEN viruses, DEN1 to DEN4, reacted with nLc4Cer, and the non-reducing terminal disaccharide residue Galß1-4GlcNAcß1- was found to be a critical determinant for the binding of DEN2. Chemically synthesized derivatives carrying multiple carbohydrate residues of nLc4, but not nLc4 oligosaccharide, inhibited DEN2 infection of BHK-21 cells. These findings strongly suggested that multivalent nLc4 oligosaccharide could act as a competitive inhibitor against the binding of DEN2 to the host cells.

* These authors contributed equally to this work and share first authorship.


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