Isolation and characterization of conglutinin as an influenza A virus inhibitor
Identifieur interne : 001F74 ( Main/Exploration ); précédent : 001F73; suivant : 001F75Isolation and characterization of conglutinin as an influenza A virus inhibitor
Auteurs : Nobutaka Wakamiya [Japon] ; Yoshinobu Okuno [Japon] ; Fuyoko Sasao [Japon] ; Shigeharu Ueda [Japon] ; Kumiko Yoshimatsu [Japon] ; Masaharu Naiki [Japon] ; Takashi Kurimura [Japon]Source :
- Biochemical and Biophysical Research Communications [ 0006-291X ] ; 1992.
English descriptors
- Teeft :
- Academic press, Animal lectins, Animal serum, Assay, Biological binding specificity, Biophysical, Biophysical research communications, Bovine, Bovine sera, Bovine serum, Carbohydrate, Carbohydrate structure, Complex carbohydrates, Conglutinin, Conglutinin activity, Conglutinin rabbit serum, Conglutinin titer, Divalent cations, Equal volume, Gradient polyacrylamide, Hemagglutinating activity, High correlation, Highest dilution, Immunoprecipitation assay, Influenza, Influenza virus, Inhibitor, Kawasaki, Lectin, Mannose residues, Microbial diseases, Microbial organisms, Nacl, Neutralizing activity, Osaka university, Other hand, Passaged, Polypeptide, Rabbit serum, Ripa buffer, Room temperature, Solubilized virus, Titer, Various influenza, Various treatments, Virus antigen.
Abstract
Abstract: Normal horse and guinea pig sera contain α2-macroglobulin which inhibits the infectivity and hemagglutinating activity of influenza A viruses of the H2 and H3 subtypes. On the other hand, normal bovine serum contains a component termed β inhibitor that inhibits the infectivity and hemagglutinating activity of influenza A viruses of the H1 and H3 subtypes. To investigate the nature of the β inhibitor of influenza A virus, we purified the conglutinin and examined its characteristics. First, we found a high correlation between the hemagglutination inhibition(HI) titer and conglutinin titer in several bovine sera(r=0.906, p<0.005). The HI of bovine serum was mainly dependent on conglutinin because the HI activity was abrogated by N-acetylglucosamine but not by D-mannose. The conglutinin, purified from bovine serum, had neutralizing-activity as well as HI activity on influenza A viruses of the H1 and H3 subtypes. The HI activity of conglutinin was heat stable(56°C, 30 min), Ca++-dependent, and resistant to both neuraminidase and periodate treatments. The HI activity of purified conglutinin was blocked by N-acetylglucosamine but not by D-mannose. The conglutinin was bound to hemagglutinin which had high mannose and complex sugar chains and its binding was inhibited by N-acetylglucosamine and dependent on divalent cations. These data indicate that the β-like inhibitor activity of bovine serum is mainly dependent on conglutinin which inhibits hemagglutination and neutralizes the virus infectivity by its binding to a carbohydrate site at the HA.
Url:
DOI: 10.1016/0006-291X(92)90440-V
Affiliations:
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Medicine, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565</wicri:regionArea><wicri:noRegion>Osaka 565</wicri:noRegion></affiliation></author><author><name sortKey="Sasao, Fuyoko" sort="Sasao, Fuyoko" uniqKey="Sasao F" first="Fuyoko" last="Sasao">Fuyoko Sasao</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Preventive Medicine, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565</wicri:regionArea><wicri:noRegion>Osaka 565</wicri:noRegion></affiliation></author><author><name sortKey="Ueda, Shigeharu" sort="Ueda, Shigeharu" uniqKey="Ueda S" first="Shigeharu" last="Ueda">Shigeharu Ueda</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Preventive Medicine, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565</wicri:regionArea><wicri:noRegion>Osaka 565</wicri:noRegion></affiliation></author><author><name sortKey="Yoshimatsu, Kumiko" sort="Yoshimatsu, Kumiko" uniqKey="Yoshimatsu K" first="Kumiko" last="Yoshimatsu">Kumiko Yoshimatsu</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Institute of Immunological Science, Hokkaido University, Sapporo, Hokkaido 060</wicri:regionArea><wicri:noRegion>Hokkaido 060</wicri:noRegion></affiliation></author><author><name sortKey="Naiki, Masaharu" sort="Naiki, Masaharu" uniqKey="Naiki M" first="Masaharu" last="Naiki">Masaharu Naiki</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Veterinary Science, National Institute of Health, Shinagawa, Tokyo 141</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Kurimura, Takashi" sort="Kurimura, Takashi" uniqKey="Kurimura T" first="Takashi" last="Kurimura">Takashi Kurimura</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Pathology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565</wicri:regionArea><wicri:noRegion>Osaka 565</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Biochemical and Biophysical Research Communications</title><title level="j" type="abbrev">YBBRC</title><idno type="ISSN">0006-291X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992">1992</date><biblScope unit="volume">187</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="1270">1270</biblScope><biblScope unit="page" to="1278">1278</biblScope></imprint><idno type="ISSN">0006-291X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-291X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Animal lectins</term><term>Animal serum</term><term>Assay</term><term>Biological binding specificity</term><term>Biophysical</term><term>Biophysical research communications</term><term>Bovine</term><term>Bovine sera</term><term>Bovine serum</term><term>Carbohydrate</term><term>Carbohydrate structure</term><term>Complex carbohydrates</term><term>Conglutinin</term><term>Conglutinin activity</term><term>Conglutinin rabbit serum</term><term>Conglutinin titer</term><term>Divalent cations</term><term>Equal volume</term><term>Gradient polyacrylamide</term><term>Hemagglutinating activity</term><term>High correlation</term><term>Highest dilution</term><term>Immunoprecipitation assay</term><term>Influenza</term><term>Influenza virus</term><term>Inhibitor</term><term>Kawasaki</term><term>Lectin</term><term>Mannose residues</term><term>Microbial diseases</term><term>Microbial organisms</term><term>Nacl</term><term>Neutralizing activity</term><term>Osaka university</term><term>Other hand</term><term>Passaged</term><term>Polypeptide</term><term>Rabbit serum</term><term>Ripa buffer</term><term>Room temperature</term><term>Solubilized virus</term><term>Titer</term><term>Various influenza</term><term>Various treatments</term><term>Virus antigen</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Normal horse and guinea pig sera contain α2-macroglobulin which inhibits the infectivity and hemagglutinating activity of influenza A viruses of the H2 and H3 subtypes. On the other hand, normal bovine serum contains a component termed β inhibitor that inhibits the infectivity and hemagglutinating activity of influenza A viruses of the H1 and H3 subtypes. To investigate the nature of the β inhibitor of influenza A virus, we purified the conglutinin and examined its characteristics. First, we found a high correlation between the hemagglutination inhibition(HI) titer and conglutinin titer in several bovine sera(r=0.906, p<0.005). The HI of bovine serum was mainly dependent on conglutinin because the HI activity was abrogated by N-acetylglucosamine but not by D-mannose. The conglutinin, purified from bovine serum, had neutralizing-activity as well as HI activity on influenza A viruses of the H1 and H3 subtypes. The HI activity of conglutinin was heat stable(56°C, 30 min), Ca++-dependent, and resistant to both neuraminidase and periodate treatments. The HI activity of purified conglutinin was blocked by N-acetylglucosamine but not by D-mannose. The conglutinin was bound to hemagglutinin which had high mannose and complex sugar chains and its binding was inhibited by N-acetylglucosamine and dependent on divalent cations. These data indicate that the β-like inhibitor activity of bovine serum is mainly dependent on conglutinin which inhibits hemagglutination and neutralizes the virus infectivity by its binding to a carbohydrate site at the HA.</div></front></TEI><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement></list><tree><country name="Japon"><noRegion><name sortKey="Wakamiya, Nobutaka" sort="Wakamiya, Nobutaka" uniqKey="Wakamiya N" first="Nobutaka" last="Wakamiya">Nobutaka Wakamiya</name></noRegion><name sortKey="Kurimura, Takashi" sort="Kurimura, Takashi" uniqKey="Kurimura T" first="Takashi" last="Kurimura">Takashi Kurimura</name><name sortKey="Naiki, Masaharu" sort="Naiki, Masaharu" uniqKey="Naiki M" first="Masaharu" last="Naiki">Masaharu Naiki</name><name sortKey="Okuno, Yoshinobu" sort="Okuno, Yoshinobu" uniqKey="Okuno Y" first="Yoshinobu" last="Okuno">Yoshinobu Okuno</name><name sortKey="Sasao, Fuyoko" sort="Sasao, Fuyoko" uniqKey="Sasao F" first="Fuyoko" last="Sasao">Fuyoko Sasao</name><name sortKey="Ueda, Shigeharu" sort="Ueda, Shigeharu" uniqKey="Ueda S" first="Shigeharu" last="Ueda">Shigeharu Ueda</name><name sortKey="Yoshimatsu, Kumiko" sort="Yoshimatsu, Kumiko" uniqKey="Yoshimatsu K" first="Kumiko" last="Yoshimatsu">Kumiko Yoshimatsu</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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