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- Takashi Suzuki
- <!--label omitted: 1-->Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 381051;
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- Allen Portner
- <!--label omitted: 1-->Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 381051;
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- Ruth Ann Scroggs
- <!--label omitted: 1-->Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 381051;
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- Makoto Uchikawa
- <!--label omitted: 4-->Central Blood Center, Japanese Red Cross, 4-1-31 Hiroo, Shibuya-ku, Tokyo 150-0012,4 Japan; and
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- Noriko Koyama
- <!--label omitted: 2-->Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Shizuoka 422-8526,2 and
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- Kazuko Matsuo
- <!--label omitted: 2-->Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Shizuoka 422-8526,2 and
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- Yasuo Suzuki
- <!--label omitted: 2-->Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Shizuoka 422-8526,2 and
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- Toru Takimoto
- <!--label omitted: 1-->Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 381051;
抄録
<jats:title>ABSTRACT</jats:title> <jats:p> Through their hemagglutinin-neuraminidase glycoprotein, parainfluenza viruses bind to sialic acid-containing glycoconjugates to initiate infection. Although the virus-receptor interaction is a key factor of infection, the exact nature of the receptors that human parainfluenza viruses recognize has not been determined. We evaluated the abilities of human parainfluenza virus types 1 (hPIV-1) and 3 (hPIV-3) to bind to different types of gangliosides. Both hPIV-1 and hPIV-3 preferentially bound to neolacto-series gangliosides containing a terminal <jats:italic>N</jats:italic> -acetylneuraminic acid (NeuAc) linked to <jats:italic>N</jats:italic> -acetyllactosamine (Galβ1-4GlcNAc) by the α2-3 linkage (NeuAcα2-3Galβ1-4GlcNAc). Unlike hPIV-1, hPIV-3 bound to gangliosides with a terminal NeuAc linked to Galβ1-4GlcNAc through an α2-6 linkage (NeuAcα2-6Galβ1-4GlcNAc) or to gangliosides with a different sialic acid, <jats:italic>N</jats:italic> -glycolylneuraminic acid (NeuGc), linked to Galβ1-4GlcNAc (NeuGcα2-3Galβ1-4GlcNAc). These results indicate that the molecular species of glycoconjugate that hPIV-1 recognizes are more limited than those recognized by hPIV-3. Further analysis using purified gangliosides revealed that the oligosaccharide core structure is also an important element for binding. Gangliosides that contain branched <jats:italic>N</jats:italic> -acetyllactosaminoglycans in their core structure showed higher avidity than those without them. Agglutination of human, cow, and guinea pig erythrocytes but not equine erythrocytes by hPIV-1 and hPIV-3 correlated well with the presence or the absence of sialic acid-linked branched <jats:italic>N</jats:italic> -acetyllactosaminoglycans on the cell surface. Finally, NeuAcα2-3I, which bound to both viruses, inhibited virus infection of Lewis lung carcinoma-monkey kidney cells in a dose-dependent manner. We conclude that hPIV-1 and hPIV-3 preferentially recognize oligosaccharides containing branched <jats:italic>N</jats:italic> -acetyllactosaminoglycans with terminal NeuAcα2-3Gal as receptors and that hPIV-3 also recognizes NeuAcα2-6Gal- or NeuGcα2-3Gal-containing receptors. These findings provide important information that can be used to develop inhibitors that prevent human parainfluenza virus infection. </jats:p>
収録刊行物
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- Journal of Virology
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Journal of Virology 75 (10), 4604-4613, 2001-05-15
American Society for Microbiology
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詳細情報 詳細情報について
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- CRID
- 1361418520569993600
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- NII論文ID
- 80012481856
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- ISSN
- 10985514
- 0022538X
- http://id.crossref.org/issn/0022538X
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