Identification of Amino Acids of Influenza Virus HA Responsible for Resistance to a Fusion Inhibitor, Stachyflin
We have recently described a novel hemagglutinin (HA) conformational change inhibitor of human influenza virus, Stachyflin (Yoshimoto et al, Arch. Virol., 144, 1-14, 1999). Stachyflin-resistant variants of human influenza A/WSN/33 (H1N1) virus were isolated in vitro and the nucleotide sequences of t...
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| Veröffentlicht in: | MICROBIOLOGY and IMMUNOLOGY 2000, Vol.44(8), pp.677-685 |
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| creator | Yoshimoto, Jun Kakui, Mayumi Iwasaki, Hiroko Sugimoto, Hirohiko Fujiwara, Tamio Hattori, Naohiko |
| description | We have recently described a novel hemagglutinin (HA) conformational change inhibitor of human influenza virus, Stachyflin (Yoshimoto et al, Arch. Virol., 144, 1-14, 1999). Stachyflin-resistant variants of human influenza A/WSN/33 (H1N1) virus were isolated in vitro and the nucleotide sequences of their HA genes were determined. The relation of amino acid substitutions and Stachyflin resistance was analyzed with in vitro membrane fusion between HA-expressing cells and octadecylrhodamine (R18)-labelled chick erythrocytes (RBC). The amino acid substitutions, lysine to arginine at position 51 or lysine to glutamic acid at position 121 of the HA2 subunit of the HA protein was enough to confer a Stachyflin-resistant phenotype of HA protein. The molecular mechanism of anti-HA conformational change activity of Stachyflin is discussed. |
| doi_str_mv | 10.1111/j.1348-0421.2000.tb02549.x |
| format | Article |
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Virol., 144, 1-14, 1999). Stachyflin-resistant variants of human influenza A/WSN/33 (H1N1) virus were isolated in vitro and the nucleotide sequences of their HA genes were determined. The relation of amino acid substitutions and Stachyflin resistance was analyzed with in vitro membrane fusion between HA-expressing cells and octadecylrhodamine (R18)-labelled chick erythrocytes (RBC). The amino acid substitutions, lysine to arginine at position 51 or lysine to glutamic acid at position 121 of the HA2 subunit of the HA protein was enough to confer a Stachyflin-resistant phenotype of HA protein. The molecular mechanism of anti-HA conformational change activity of Stachyflin is discussed.</description><identifier>ISSN: 0385-5600</identifier><identifier>EISSN: 1348-0421</identifier><identifier>DOI: 10.1111/j.1348-0421.2000.tb02549.x</identifier><identifier>PMID: 11021398</identifier><identifier>CODEN: MIIMDV</identifier><language>eng</language><publisher>Tokyo: Blackwell Publishing Ltd</publisher><subject>Amino Acid Substitution ; Amino Acids - physiology ; Animals ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antiviral agents ; Antiviral Agents - pharmacology ; Biological and medical sciences ; Cattle ; Cell Fusion ; Cell Line ; Chickens ; DNA Mutational Analysis ; Dogs ; Fusion inhibitor ; Genes, Viral ; Hemagglutinin Glycoproteins, Influenza Virus - genetics ; Hemagglutinin Glycoproteins, Influenza Virus - physiology ; Influenza A virus ; Influenza A virus - drug effects ; Influenza A virus - genetics ; Influenza A virus - pathogenicity ; Influenza virus ; Medical sciences ; Models, Molecular ; Pharmacology. 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Virol., 144, 1-14, 1999). Stachyflin-resistant variants of human influenza A/WSN/33 (H1N1) virus were isolated in vitro and the nucleotide sequences of their HA genes were determined. The relation of amino acid substitutions and Stachyflin resistance was analyzed with in vitro membrane fusion between HA-expressing cells and octadecylrhodamine (R18)-labelled chick erythrocytes (RBC). The amino acid substitutions, lysine to arginine at position 51 or lysine to glutamic acid at position 121 of the HA2 subunit of the HA protein was enough to confer a Stachyflin-resistant phenotype of HA protein. The molecular mechanism of anti-HA conformational change activity of Stachyflin is discussed.</description><subject>Amino Acid Substitution</subject><subject>Amino Acids - physiology</subject><subject>Animals</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antiviral agents</subject><subject>Antiviral Agents - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Cell Fusion</subject><subject>Cell Line</subject><subject>Chickens</subject><subject>DNA Mutational Analysis</subject><subject>Dogs</subject><subject>Fusion inhibitor</subject><subject>Genes, Viral</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - genetics</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - physiology</subject><subject>Influenza A virus</subject><subject>Influenza A virus - drug effects</subject><subject>Influenza A virus - genetics</subject><subject>Influenza A virus - pathogenicity</subject><subject>Influenza virus</subject><subject>Medical sciences</subject><subject>Models, Molecular</subject><subject>Pharmacology. 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Antiinfectious agents. Antiparasitic agents</topic><topic>Antiviral agents</topic><topic>Antiviral Agents - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Cell Fusion</topic><topic>Cell Line</topic><topic>Chickens</topic><topic>DNA Mutational Analysis</topic><topic>Dogs</topic><topic>Fusion inhibitor</topic><topic>Genes, Viral</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - genetics</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - physiology</topic><topic>Influenza A virus</topic><topic>Influenza A virus - drug effects</topic><topic>Influenza A virus - genetics</topic><topic>Influenza A virus - pathogenicity</topic><topic>Influenza virus</topic><topic>Medical sciences</topic><topic>Models, Molecular</topic><topic>Pharmacology. Drug treatments</topic><topic>Sesquiterpenes - pharmacology</topic><topic>Stachyflin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yoshimoto, Jun</creatorcontrib><creatorcontrib>Kakui, Mayumi</creatorcontrib><creatorcontrib>Iwasaki, Hiroko</creatorcontrib><creatorcontrib>Sugimoto, Hirohiko</creatorcontrib><creatorcontrib>Fujiwara, Tamio</creatorcontrib><creatorcontrib>Hattori, Naohiko</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>MICROBIOLOGY and IMMUNOLOGY</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yoshimoto, Jun</au><au>Kakui, Mayumi</au><au>Iwasaki, Hiroko</au><au>Sugimoto, Hirohiko</au><au>Fujiwara, Tamio</au><au>Hattori, Naohiko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of Amino Acids of Influenza Virus HA Responsible for Resistance to a Fusion Inhibitor, Stachyflin</atitle><jtitle>MICROBIOLOGY and IMMUNOLOGY</jtitle><addtitle>Microbiology and Immunology</addtitle><date>2000-01-01</date><risdate>2000</risdate><volume>44</volume><issue>8</issue><spage>677</spage><epage>685</epage><pages>677-685</pages><issn>0385-5600</issn><eissn>1348-0421</eissn><coden>MIIMDV</coden><abstract>We have recently described a novel hemagglutinin (HA) conformational change inhibitor of human influenza virus, Stachyflin (Yoshimoto et al, Arch. Virol., 144, 1-14, 1999). Stachyflin-resistant variants of human influenza A/WSN/33 (H1N1) virus were isolated in vitro and the nucleotide sequences of their HA genes were determined. The relation of amino acid substitutions and Stachyflin resistance was analyzed with in vitro membrane fusion between HA-expressing cells and octadecylrhodamine (R18)-labelled chick erythrocytes (RBC). The amino acid substitutions, lysine to arginine at position 51 or lysine to glutamic acid at position 121 of the HA2 subunit of the HA protein was enough to confer a Stachyflin-resistant phenotype of HA protein. The molecular mechanism of anti-HA conformational change activity of Stachyflin is discussed.</abstract><cop>Tokyo</cop><pub>Blackwell Publishing Ltd</pub><pmid>11021398</pmid><doi>10.1111/j.1348-0421.2000.tb02549.x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Substitution Amino Acids - physiology Animals Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral agents Antiviral Agents - pharmacology Biological and medical sciences Cattle Cell Fusion Cell Line Chickens DNA Mutational Analysis Dogs Fusion inhibitor Genes, Viral Hemagglutinin Glycoproteins, Influenza Virus - genetics Hemagglutinin Glycoproteins, Influenza Virus - physiology Influenza A virus Influenza A virus - drug effects Influenza A virus - genetics Influenza A virus - pathogenicity Influenza virus Medical sciences Models, Molecular Pharmacology. Drug treatments Sesquiterpenes - pharmacology Stachyflin |
| title | Identification of Amino Acids of Influenza Virus HA Responsible for Resistance to a Fusion Inhibitor, Stachyflin |
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