A highly attenuated rabies virus HEP-Flury strain reverts to virulent by single amino acid substitution to arginine at position 333 in glycoprotein
An amino acid at position 333 in the glycoprotein of several fixed rabies virus strains is responsible for the pathogenicity in adult mice. Substitution of arginine at this position largely reduces the viral pathogenicity in adult mice. Attenuation by this single amino acid substitution has been est...
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| Veröffentlicht in: | Virus research 2006-08, Vol.119 (2), p.208-215 |
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| creator | Takayama-Ito, Mutsuyo Inoue, Ken-ichi Shoji, Yoko Inoue, Satoshi Iijima, Toshio Sakai, Takeo Kurane, Ichiro Morimoto, Kinjiro |
| description | An amino acid at position 333 in the glycoprotein of several fixed rabies virus strains is responsible for the pathogenicity in adult mice. Substitution of arginine at this position largely reduces the viral pathogenicity in adult mice. Attenuation by this single amino acid substitution has been established by using escape mutants selected by monoclonal antibodies and point-mutated virus generated by reverse-genetics. A highly attenuated HEP-Flury strain, which was selected by serial passages in cell cultures, has glutamine at this position. In this study, a point-mutated rHEP
333R virus, having arginine at position 333, was generated and examined for the responsibility of this substitution in rabies pathogenicity. The rHEP
333R acquired an ability to spread and propagate in mouse brain but the parental rHEP did not. The pathogenicity of rHEP
333R to adult mice by intracerebral inoculation largely increased. We confirmed that an arginine at position 333 contributed to reversion of the pathogenicity in a highly attenuated HEP-Flury strain. |
| doi_str_mv | 10.1016/j.virusres.2006.01.014 |
| format | Article |
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333R virus, having arginine at position 333, was generated and examined for the responsibility of this substitution in rabies pathogenicity. The rHEP
333R acquired an ability to spread and propagate in mouse brain but the parental rHEP did not. The pathogenicity of rHEP
333R to adult mice by intracerebral inoculation largely increased. We confirmed that an arginine at position 333 contributed to reversion of the pathogenicity in a highly attenuated HEP-Flury strain.</description><identifier>ISSN: 0168-1702</identifier><identifier>EISSN: 1872-7492</identifier><identifier>DOI: 10.1016/j.virusres.2006.01.014</identifier><identifier>PMID: 16473429</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Substitution ; Animals ; Antibodies, Viral - blood ; Antigens, Viral - genetics ; Antigens, Viral - physiology ; Arginine - genetics ; Arginine - physiology ; Brain - virology ; Disease Models, Animal ; Glycoprotein ; Glycoproteins - genetics ; Glycoproteins - physiology ; Mice ; Mutation ; Neutralization Tests ; Pathogenicity ; Rabies - virology ; Rabies virus ; Rabies virus - genetics ; Rabies virus - pathogenicity ; Rats ; Suppression, Genetic - genetics ; Survival Analysis ; Viral Envelope Proteins - genetics ; Viral Envelope Proteins - physiology</subject><ispartof>Virus research, 2006-08, Vol.119 (2), p.208-215</ispartof><rights>2006 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-e3786a94c1551b27d8fc2f4f37eb9da9adba31ba35f39cdf762671a06f74bb93</citedby><cites>FETCH-LOGICAL-c463t-e3786a94c1551b27d8fc2f4f37eb9da9adba31ba35f39cdf762671a06f74bb93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.virusres.2006.01.014$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16473429$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Takayama-Ito, Mutsuyo</creatorcontrib><creatorcontrib>Inoue, Ken-ichi</creatorcontrib><creatorcontrib>Shoji, Yoko</creatorcontrib><creatorcontrib>Inoue, Satoshi</creatorcontrib><creatorcontrib>Iijima, Toshio</creatorcontrib><creatorcontrib>Sakai, Takeo</creatorcontrib><creatorcontrib>Kurane, Ichiro</creatorcontrib><creatorcontrib>Morimoto, Kinjiro</creatorcontrib><title>A highly attenuated rabies virus HEP-Flury strain reverts to virulent by single amino acid substitution to arginine at position 333 in glycoprotein</title><title>Virus research</title><addtitle>Virus Res</addtitle><description>An amino acid at position 333 in the glycoprotein of several fixed rabies virus strains is responsible for the pathogenicity in adult mice. Substitution of arginine at this position largely reduces the viral pathogenicity in adult mice. Attenuation by this single amino acid substitution has been established by using escape mutants selected by monoclonal antibodies and point-mutated virus generated by reverse-genetics. A highly attenuated HEP-Flury strain, which was selected by serial passages in cell cultures, has glutamine at this position. In this study, a point-mutated rHEP
333R virus, having arginine at position 333, was generated and examined for the responsibility of this substitution in rabies pathogenicity. The rHEP
333R acquired an ability to spread and propagate in mouse brain but the parental rHEP did not. The pathogenicity of rHEP
333R to adult mice by intracerebral inoculation largely increased. We confirmed that an arginine at position 333 contributed to reversion of the pathogenicity in a highly attenuated HEP-Flury strain.</description><subject>Amino Acid Substitution</subject><subject>Animals</subject><subject>Antibodies, Viral - blood</subject><subject>Antigens, Viral - genetics</subject><subject>Antigens, Viral - physiology</subject><subject>Arginine - genetics</subject><subject>Arginine - physiology</subject><subject>Brain - virology</subject><subject>Disease Models, Animal</subject><subject>Glycoprotein</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - physiology</subject><subject>Mice</subject><subject>Mutation</subject><subject>Neutralization Tests</subject><subject>Pathogenicity</subject><subject>Rabies - virology</subject><subject>Rabies virus</subject><subject>Rabies virus - genetics</subject><subject>Rabies virus - pathogenicity</subject><subject>Rats</subject><subject>Suppression, Genetic - genetics</subject><subject>Survival Analysis</subject><subject>Viral Envelope Proteins - genetics</subject><subject>Viral Envelope Proteins - physiology</subject><issn>0168-1702</issn><issn>1872-7492</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkdtq3DAQhkVoabZpXyHoqnfe6mTJvmsIOUGgvci9kOXxZhavvJHkhX2OvnC0h9LLwAjB6Jv5QR8h15wtOeP653q5wzinCGkpGNNLxkupC7LgjRGVUa34RBYFbCpumLgkX1NaswJKo7-QS66VkUq0C_L3hr7i6nXcU5czhNll6Gl0HUKixwT6ePenuh_nuKcpR4eBRthBzInm6UiMEDLtyiuG1QjUbTBM1HnsaZq7lDHPGadwoF1cYcBQmEy3U8JjX0pJy9LVuPfTNk4ZMHwjnwc3Jvh-vq_Iy_3dy-1j9fz74en25rnySstcgTSNdq3yvK55J0zfDF4MapAGurZ3res7J3k59SBb3w9GC224Y3owqutaeUV-nNaW2LcZUrYbTB7G0QWY5mR1w4RRsv4Q5EZwVTeigPoE-jil4maw24gbF_eWM3vQZtf2nzZ70GYZL6XK4PU5Ye420P8fO3sqwK8TAOU_dgjRJo8QPPQYwWfbT_hRxjuwdrBy</recordid><startdate>20060801</startdate><enddate>20060801</enddate><creator>Takayama-Ito, Mutsuyo</creator><creator>Inoue, Ken-ichi</creator><creator>Shoji, Yoko</creator><creator>Inoue, Satoshi</creator><creator>Iijima, Toshio</creator><creator>Sakai, Takeo</creator><creator>Kurane, Ichiro</creator><creator>Morimoto, Kinjiro</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20060801</creationdate><title>A highly attenuated rabies virus HEP-Flury strain reverts to virulent by single amino acid substitution to arginine at position 333 in glycoprotein</title><author>Takayama-Ito, Mutsuyo ; Inoue, Ken-ichi ; Shoji, Yoko ; Inoue, Satoshi ; Iijima, Toshio ; Sakai, Takeo ; Kurane, Ichiro ; Morimoto, Kinjiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-e3786a94c1551b27d8fc2f4f37eb9da9adba31ba35f39cdf762671a06f74bb93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Substitution</topic><topic>Animals</topic><topic>Antibodies, Viral - blood</topic><topic>Antigens, Viral - genetics</topic><topic>Antigens, Viral - physiology</topic><topic>Arginine - genetics</topic><topic>Arginine - physiology</topic><topic>Brain - virology</topic><topic>Disease Models, Animal</topic><topic>Glycoprotein</topic><topic>Glycoproteins - genetics</topic><topic>Glycoproteins - physiology</topic><topic>Mice</topic><topic>Mutation</topic><topic>Neutralization Tests</topic><topic>Pathogenicity</topic><topic>Rabies - virology</topic><topic>Rabies virus</topic><topic>Rabies virus - genetics</topic><topic>Rabies virus - pathogenicity</topic><topic>Rats</topic><topic>Suppression, Genetic - genetics</topic><topic>Survival Analysis</topic><topic>Viral Envelope Proteins - genetics</topic><topic>Viral Envelope Proteins - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takayama-Ito, Mutsuyo</creatorcontrib><creatorcontrib>Inoue, Ken-ichi</creatorcontrib><creatorcontrib>Shoji, Yoko</creatorcontrib><creatorcontrib>Inoue, Satoshi</creatorcontrib><creatorcontrib>Iijima, Toshio</creatorcontrib><creatorcontrib>Sakai, Takeo</creatorcontrib><creatorcontrib>Kurane, Ichiro</creatorcontrib><creatorcontrib>Morimoto, Kinjiro</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Virus research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takayama-Ito, Mutsuyo</au><au>Inoue, Ken-ichi</au><au>Shoji, Yoko</au><au>Inoue, Satoshi</au><au>Iijima, Toshio</au><au>Sakai, Takeo</au><au>Kurane, Ichiro</au><au>Morimoto, Kinjiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A highly attenuated rabies virus HEP-Flury strain reverts to virulent by single amino acid substitution to arginine at position 333 in glycoprotein</atitle><jtitle>Virus research</jtitle><addtitle>Virus Res</addtitle><date>2006-08-01</date><risdate>2006</risdate><volume>119</volume><issue>2</issue><spage>208</spage><epage>215</epage><pages>208-215</pages><issn>0168-1702</issn><eissn>1872-7492</eissn><abstract>An amino acid at position 333 in the glycoprotein of several fixed rabies virus strains is responsible for the pathogenicity in adult mice. Substitution of arginine at this position largely reduces the viral pathogenicity in adult mice. Attenuation by this single amino acid substitution has been established by using escape mutants selected by monoclonal antibodies and point-mutated virus generated by reverse-genetics. A highly attenuated HEP-Flury strain, which was selected by serial passages in cell cultures, has glutamine at this position. In this study, a point-mutated rHEP
333R virus, having arginine at position 333, was generated and examined for the responsibility of this substitution in rabies pathogenicity. The rHEP
333R acquired an ability to spread and propagate in mouse brain but the parental rHEP did not. The pathogenicity of rHEP
333R to adult mice by intracerebral inoculation largely increased. We confirmed that an arginine at position 333 contributed to reversion of the pathogenicity in a highly attenuated HEP-Flury strain.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>16473429</pmid><doi>10.1016/j.virusres.2006.01.014</doi><tpages>8</tpages></addata></record> |
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| ispartof | Virus research, 2006-08, Vol.119 (2), p.208-215 |
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| subjects | Amino Acid Substitution Animals Antibodies, Viral - blood Antigens, Viral - genetics Antigens, Viral - physiology Arginine - genetics Arginine - physiology Brain - virology Disease Models, Animal Glycoprotein Glycoproteins - genetics Glycoproteins - physiology Mice Mutation Neutralization Tests Pathogenicity Rabies - virology Rabies virus Rabies virus - genetics Rabies virus - pathogenicity Rats Suppression, Genetic - genetics Survival Analysis Viral Envelope Proteins - genetics Viral Envelope Proteins - physiology |
| title | A highly attenuated rabies virus HEP-Flury strain reverts to virulent by single amino acid substitution to arginine at position 333 in glycoprotein |
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