A Unique Phosphatidylinositol Bearing a Novel Branched-Chain Fatty Acid from Rhodococcus equi Binds to Influenza Virus Hemagglutinin and Inhibits the Infection of Cells
Identifieur interne : 001852 ( Main/Exploration ); précédent : 001851; suivant : 001853A Unique Phosphatidylinositol Bearing a Novel Branched-Chain Fatty Acid from Rhodococcus equi Binds to Influenza Virus Hemagglutinin and Inhibits the Infection of Cells
Auteurs : Chao-Tan Guo ; Shinji Ohta ; Akihiro Yoshimoto [Hong Kong] ; Kuniho Nakata ; Kennedy Francis Shortridge [Hong Kong] ; Tadanobu Takahashi ; Takashi Suzuki ; Daisei Miyamoto ; Kazuya I.-P. Jwa Hidari ; Yasuo SuzukiSource :
- The Journal of Biochemistry [ 0021-924X ] ; 2001.
Abstract
From the aquatic bacterium Rhodococcus equi strain S420, we isolated a substance that strongly binds to influenza viruses. Structural analyses revealed that it is a unique type of phosphatidylinositol (Ptdlns) bearing a branched-chain fatty acid (14-methyloctade-canoic acid). In a TLC/virus-binding immunostaining assay, this Ptdlns bound to all subtypes of hemagglutinin (HA) of influenza A viruses tested, isolated from humans, ducks and swine, and also to human influenza B viruses. Furthermore, the Ptdlns significantly prevented the infection of MDCK cells by influenza viruses, and also inhibited the virus-mediated hemagglutination and low pH-induced hemolysis of human erythrocytes, which represents the fusogenic activities of the viral HA. We also used purified hemagglutinin instead of virions to examine the interaction between viral HA and Ptdlns, showing that the Ptdlns binds to hemagglutinin. These findings indicate that the inhibitory mechanism of Ptdlns on the influenza virus infection may be through its binding to viral HA spikes and host cell endosomal/lysosomal membranes, which are mediated by the function of viral HA.
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DOI: 10.1093/oxfordjournals.jbchem.a002996
Affiliations:
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Jwa Hidari</name><affiliation><wicri:noCountry code="subField">422-8526</wicri:noCountry></affiliation></author><author><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name><affiliation></affiliation><affiliation></affiliation><affiliation><wicri:noCountry code="subField">ac.jp</wicri:noCountry></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">The Journal of Biochemistry</title><idno type="eISSN">-</idno><idno type="ISSN">0021-924X</idno><imprint><publisher>Oxford University Press</publisher><date when="2001-09">2001</date><biblScope unit="vol">130</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="377">377</biblScope><biblScope unit="page" to="384">384</biblScope></imprint><idno type="ISSN">0021-924X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-924X</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">From the aquatic bacterium Rhodococcus equi strain S420, we isolated a substance that strongly binds to influenza viruses. Structural analyses revealed that it is a unique type of phosphatidylinositol (Ptdlns) bearing a branched-chain fatty acid (14-methyloctade-canoic acid). In a TLC/virus-binding immunostaining assay, this Ptdlns bound to all subtypes of hemagglutinin (HA) of influenza A viruses tested, isolated from humans, ducks and swine, and also to human influenza B viruses. Furthermore, the Ptdlns significantly prevented the infection of MDCK cells by influenza viruses, and also inhibited the virus-mediated hemagglutination and low pH-induced hemolysis of human erythrocytes, which represents the fusogenic activities of the viral HA. We also used purified hemagglutinin instead of virions to examine the interaction between viral HA and Ptdlns, showing that the Ptdlns binds to hemagglutinin. These findings indicate that the inhibitory mechanism of Ptdlns on the influenza virus infection may be through its binding to viral HA spikes and host cell endosomal/lysosomal membranes, which are mediated by the function of viral HA.</div></front></TEI><affiliations><list><country><li>Hong Kong</li></country></list><tree><noCountry><name sortKey="Guo, Chao Tan" sort="Guo, Chao Tan" uniqKey="Guo C" first="Chao-Tan" last="Guo">Chao-Tan Guo</name><name sortKey="Hidari, Kazuya I P Jwa" sort="Hidari, Kazuya I P Jwa" uniqKey="Hidari K" first="Kazuya I.-P. Jwa" last="Hidari">Kazuya I.-P. Jwa Hidari</name><name sortKey="Miyamoto, Daisei" sort="Miyamoto, Daisei" uniqKey="Miyamoto D" first="Daisei" last="Miyamoto">Daisei Miyamoto</name><name sortKey="Nakata, Kuniho" sort="Nakata, Kuniho" uniqKey="Nakata K" first="Kuniho" last="Nakata">Kuniho Nakata</name><name sortKey="Ohta, Shinji" sort="Ohta, Shinji" uniqKey="Ohta S" first="Shinji" last="Ohta">Shinji Ohta</name><name sortKey="Suzuki, Takashi" sort="Suzuki, Takashi" uniqKey="Suzuki T" first="Takashi" last="Suzuki">Takashi Suzuki</name><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name><name sortKey="Takahashi, Tadanobu" sort="Takahashi, Tadanobu" uniqKey="Takahashi T" first="Tadanobu" last="Takahashi">Tadanobu Takahashi</name></noCountry><country name="Hong Kong"><noRegion><name sortKey="Yoshimoto, Akihiro" sort="Yoshimoto, Akihiro" uniqKey="Yoshimoto A" first="Akihiro" last="Yoshimoto">Akihiro Yoshimoto</name></noRegion><name sortKey="Shortridge, Kennedy Francis" sort="Shortridge, Kennedy Francis" uniqKey="Shortridge K" first="Kennedy Francis" last="Shortridge">Kennedy Francis Shortridge</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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