New ganglioside analogs that inhibit influenze virus sialidase
Identifieur interne : 000315 ( Istex/Curation ); précédent : 000314; suivant : 000316New ganglioside analogs that inhibit influenze virus sialidase
Auteurs : Yasuo Suzuki [Japon] ; Katsuhiko Sato [Japon] ; Makoto Kiso [Japon] ; Akira Hasegawa [Japon]Source :
- Glycoconjugate Journal [ 0282-0080 ] ; 1990-07-01.
English descriptors
- KwdEn :
- Teeft :
- Active site, Analog, Arthrobacter ureafaciens, Bacterial sialidase, Bacterial sialidases, Biochemical nomenclature, Biochim biophys acta, Biol chem, Carbohydr chem, Chem, Clostridium perfringens, Different subtypes, Dixon plot, Effective detergent, Enzyme activity, Enzyme preparation, Final concentration, Ganglioside, Ganglioside analogs, Gangliosides, Glycoprotein, Influenza, Influenza virus, Influenza virus sialidase, Influenza viruses, Inhibitor, Inhibitor concentration, Inhibitory activity, Matsumoto, Neu5ac, Newcastle disease virus, Nmol, Perfringens, Potent inhibitor, Reaction mixtures, Same buffer, Scientific research, Several kinds, Sialic, Sialic acid, Sialidase, Sialidase inhibitor, Sialidases, Sodium acetate buffer, Sodium taurodeoxycholate, Spike glycoprotein, Suzuki, Thioglycoside, Thioglycoside analogs, Ureafaciens, Viral, Viral membranes, Viral sialidase, Virology.
Abstract
Abstract: Synthetic thioglycoside-analogs of gangliosides such as Neu5Acα)2-S-6)Glcβ-(1-1)Ceramide (1) and the GM3 analog Neu5Acα(2-S-6)Galβ-(1–4)Glcβ(1-1)Ceramide (2), competitively inhibited GM3 hydrolysis by the sialidase of different subtypes of human and animal influenza viruses with an apparent Ki value of 2.8×10−6 and 1.5×10−5 M, respectively. The inhibitory activity of the ganglioside GM4 analog [Neu5Acα-(2-S-6)Galβ-(1-1)Ceramide (3)], in which the glucose of 1 was substituted by galactose, was lower than that of 1 (Ki =1.0×10−4 M). The thioglycoside-analogs (1, 2, 3) of the gangliosides were nonhydrolyzable substrates for influenza virus sialidase. The inhibitory activity of 1 to bacterial sialidases fromClostridium perfringens andArthrobacter ureafaciens was considerably lower than that to influenza virus sialidase, indicating that the structure of the active site in bacterial and influenza virus sialidase may be different and the analogs may be useful to determine the orientation of the substrate to the active site of sialidases, especially of influenza viruses.
Url:
DOI: 10.1007/BF01073378
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Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, 395 Yada, 422, Shizuoka</wicri:regionArea></affiliation></author><author><name sortKey="Kiso, Makoto" sort="Kiso, Makoto" uniqKey="Kiso M" first="Makoto" last="Kiso">Makoto Kiso</name><affiliation wicri:level="1"><mods:affiliation>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu</wicri:regionArea></affiliation></author><author><name sortKey="Hasegawa, Akira" sort="Hasegawa, Akira" uniqKey="Hasegawa A" first="Akira" last="Hasegawa">Akira Hasegawa</name><affiliation wicri:level="1"><mods:affiliation>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu, Japan</mods:affiliation><country 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wicri:level="1"><mods:affiliation>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, 395 Yada, 422, Shizuoka, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, 395 Yada, 422, Shizuoka</wicri:regionArea></affiliation></author><author><name sortKey="Sato, Katsuhiko" sort="Sato, Katsuhiko" uniqKey="Sato K" first="Katsuhiko" last="Sato">Katsuhiko Sato</name><affiliation wicri:level="1"><mods:affiliation>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, 395 Yada, 422, Shizuoka, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, 395 Yada, 422, Shizuoka</wicri:regionArea></affiliation></author><author><name sortKey="Kiso, Makoto" sort="Kiso, Makoto" uniqKey="Kiso M" first="Makoto" last="Kiso">Makoto Kiso</name><affiliation wicri:level="1"><mods:affiliation>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu</wicri:regionArea></affiliation></author><author><name sortKey="Hasegawa, Akira" sort="Hasegawa, Akira" uniqKey="Hasegawa A" first="Akira" last="Hasegawa">Akira Hasegawa</name><affiliation wicri:level="1"><mods:affiliation>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Glycoconjugate Journal</title><title level="j" type="sub">Official Journal of the International Glycoconjugate Organization</title><title level="j" type="abbrev">Glycoconjugate J</title><idno type="ISSN">0282-0080</idno><idno type="eISSN">1573-4986</idno><imprint><publisher>Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><date type="published" when="1990-07-01">1990-07-01</date><biblScope unit="volume">7</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="349">349</biblScope><biblScope unit="page" to="356">356</biblScope></imprint><idno type="ISSN">0282-0080</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0282-0080</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Thioglycoside-analog of ganglioside</term><term>influenza virus</term><term>sialidase inhibitor</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Active site</term><term>Analog</term><term>Arthrobacter ureafaciens</term><term>Bacterial sialidase</term><term>Bacterial sialidases</term><term>Biochemical nomenclature</term><term>Biochim biophys acta</term><term>Biol chem</term><term>Carbohydr chem</term><term>Chem</term><term>Clostridium perfringens</term><term>Different subtypes</term><term>Dixon plot</term><term>Effective detergent</term><term>Enzyme activity</term><term>Enzyme preparation</term><term>Final concentration</term><term>Ganglioside</term><term>Ganglioside analogs</term><term>Gangliosides</term><term>Glycoprotein</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus sialidase</term><term>Influenza viruses</term><term>Inhibitor</term><term>Inhibitor concentration</term><term>Inhibitory activity</term><term>Matsumoto</term><term>Neu5ac</term><term>Newcastle disease virus</term><term>Nmol</term><term>Perfringens</term><term>Potent inhibitor</term><term>Reaction mixtures</term><term>Same buffer</term><term>Scientific research</term><term>Several kinds</term><term>Sialic</term><term>Sialic acid</term><term>Sialidase</term><term>Sialidase inhibitor</term><term>Sialidases</term><term>Sodium acetate buffer</term><term>Sodium taurodeoxycholate</term><term>Spike glycoprotein</term><term>Suzuki</term><term>Thioglycoside</term><term>Thioglycoside analogs</term><term>Ureafaciens</term><term>Viral</term><term>Viral membranes</term><term>Viral sialidase</term><term>Virology</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Synthetic thioglycoside-analogs of gangliosides such as Neu5Acα)2-S-6)Glcβ-(1-1)Ceramide (1) and the GM3 analog Neu5Acα(2-S-6)Galβ-(1–4)Glcβ(1-1)Ceramide (2), competitively inhibited GM3 hydrolysis by the sialidase of different subtypes of human and animal influenza viruses with an apparent Ki value of 2.8×10−6 and 1.5×10−5 M, respectively. The inhibitory activity of the ganglioside GM4 analog [Neu5Acα-(2-S-6)Galβ-(1-1)Ceramide (3)], in which the glucose of 1 was substituted by galactose, was lower than that of 1 (Ki =1.0×10−4 M). The thioglycoside-analogs (1, 2, 3) of the gangliosides were nonhydrolyzable substrates for influenza virus sialidase. The inhibitory activity of 1 to bacterial sialidases fromClostridium perfringens andArthrobacter ureafaciens was considerably lower than that to influenza virus sialidase, indicating that the structure of the active site in bacterial and influenza virus sialidase may be different and the analogs may be useful to determine the orientation of the substrate to the active site of sialidases, especially of influenza viruses.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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