Structural basis for oseltamivir resistance of influenza viruses
Abstract Oseltamivir, one of the two anti-neuraminidase drugs, is currently the most widely used drug against influenza. Resistance to the drug has occurred infrequently among different viruses in response to drug treatment, including A H5N1 viruses, but most notably has emerged among recently circu...
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| Veröffentlicht in: | Vaccine 2009-10, Vol.27 (45), p.6317-6323 |
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| container_title | Vaccine |
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| creator | Collins, P.J Haire, L.F Lin, Y.P Liu, J Russell, R.J Walker, P.A Martin, S.R Daniels, R.S Gregory, V Skehel, J.J Gamblin, S.J Hay, A.J |
| description | Abstract Oseltamivir, one of the two anti-neuraminidase drugs, is currently the most widely used drug against influenza. Resistance to the drug has occurred infrequently among different viruses in response to drug treatment, including A H5N1 viruses, but most notably has emerged among recently circulating A H1N1 viruses and has spread throughout the population in the absence of drug use. Crystal structures of enzyme–drug complexes, together with enzymatic properties, of mutants of H5N1 neuraminidase have provided explanations for high level oseltamivir resistance due to the common H275Y mutation, with retention of zanamivir susceptibility, and intermediate level resistance due to the N295S mutation. Complementation of enhanced NA activity due to a D344N mutation by the H275Y mutation suggests an explanation for the recent emergence and predominance of oseltamivir-resistant influenza A H1N1 viruses. |
| doi_str_mv | 10.1016/j.vaccine.2009.07.017 |
| format | Article |
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Resistance to the drug has occurred infrequently among different viruses in response to drug treatment, including A H5N1 viruses, but most notably has emerged among recently circulating A H1N1 viruses and has spread throughout the population in the absence of drug use. Crystal structures of enzyme–drug complexes, together with enzymatic properties, of mutants of H5N1 neuraminidase have provided explanations for high level oseltamivir resistance due to the common H275Y mutation, with retention of zanamivir susceptibility, and intermediate level resistance due to the N295S mutation. Complementation of enhanced NA activity due to a D344N mutation by the H275Y mutation suggests an explanation for the recent emergence and predominance of oseltamivir-resistant influenza A H1N1 viruses.</description><identifier>ISSN: 0264-410X</identifier><identifier>EISSN: 1873-2518</identifier><identifier>DOI: 10.1016/j.vaccine.2009.07.017</identifier><identifier>PMID: 19840667</identifier><language>eng</language><publisher>Netherlands: Elsevier Ltd</publisher><subject>Allergy and Immunology ; Avian flu ; Crystal structure ; Drug resistance ; Drug Resistance, Viral ; Drugs ; Enzymes ; Exo-a-sialidase ; H275Y mutation ; Influenza A ; Influenza A Virus, H1N1 Subtype - drug effects ; Influenza A Virus, H1N1 Subtype - genetics ; Influenza A Virus, H5N1 Subtype - drug effects ; Influenza A Virus, H5N1 Subtype - genetics ; Influenza H5N1 ; Models, Molecular ; Mutation ; Neuraminidase - genetics ; Oseltamivir ; Oseltamivir - chemistry ; Oseltamivir - pharmacology ; Oseltamivir resistance ; Protein Structure, Tertiary ; Studies ; Swine flu ; Viral Proteins - genetics ; Viruses ; Zanamivir</subject><ispartof>Vaccine, 2009-10, Vol.27 (45), p.6317-6323</ispartof><rights>Elsevier Ltd</rights><rights>2009 Elsevier Ltd</rights><rights>Copyright Elsevier Limited Oct 23, 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-e68f22ac11b1047214133eb57e7f85d3243bd67639f88b5c728d55ba7658275d3</citedby><cites>FETCH-LOGICAL-c557t-e68f22ac11b1047214133eb57e7f85d3243bd67639f88b5c728d55ba7658275d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.proquest.com/docview/1618905352?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976,64364,64366,64368,72218</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19840667$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Collins, P.J</creatorcontrib><creatorcontrib>Haire, L.F</creatorcontrib><creatorcontrib>Lin, Y.P</creatorcontrib><creatorcontrib>Liu, J</creatorcontrib><creatorcontrib>Russell, R.J</creatorcontrib><creatorcontrib>Walker, P.A</creatorcontrib><creatorcontrib>Martin, S.R</creatorcontrib><creatorcontrib>Daniels, R.S</creatorcontrib><creatorcontrib>Gregory, V</creatorcontrib><creatorcontrib>Skehel, J.J</creatorcontrib><creatorcontrib>Gamblin, S.J</creatorcontrib><creatorcontrib>Hay, A.J</creatorcontrib><title>Structural basis for oseltamivir resistance of influenza viruses</title><title>Vaccine</title><addtitle>Vaccine</addtitle><description>Abstract Oseltamivir, one of the two anti-neuraminidase drugs, is currently the most widely used drug against influenza. Resistance to the drug has occurred infrequently among different viruses in response to drug treatment, including A H5N1 viruses, but most notably has emerged among recently circulating A H1N1 viruses and has spread throughout the population in the absence of drug use. Crystal structures of enzyme–drug complexes, together with enzymatic properties, of mutants of H5N1 neuraminidase have provided explanations for high level oseltamivir resistance due to the common H275Y mutation, with retention of zanamivir susceptibility, and intermediate level resistance due to the N295S mutation. Complementation of enhanced NA activity due to a D344N mutation by the H275Y mutation suggests an explanation for the recent emergence and predominance of oseltamivir-resistant influenza A H1N1 viruses.</description><subject>Allergy and Immunology</subject><subject>Avian flu</subject><subject>Crystal structure</subject><subject>Drug resistance</subject><subject>Drug Resistance, Viral</subject><subject>Drugs</subject><subject>Enzymes</subject><subject>Exo-a-sialidase</subject><subject>H275Y mutation</subject><subject>Influenza A</subject><subject>Influenza A Virus, H1N1 Subtype - drug effects</subject><subject>Influenza A Virus, H1N1 Subtype - genetics</subject><subject>Influenza A Virus, H5N1 Subtype - drug effects</subject><subject>Influenza A Virus, H5N1 Subtype - genetics</subject><subject>Influenza H5N1</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>Neuraminidase - genetics</subject><subject>Oseltamivir</subject><subject>Oseltamivir - chemistry</subject><subject>Oseltamivir - pharmacology</subject><subject>Oseltamivir resistance</subject><subject>Protein Structure, Tertiary</subject><subject>Studies</subject><subject>Swine flu</subject><subject>Viral Proteins - genetics</subject><subject>Viruses</subject><subject>Zanamivir</subject><issn>0264-410X</issn><issn>1873-2518</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkt9r1TAUx4M43HX6JygFQZ9az0maH31xylA3GPgwBd9Cmp5Crr3tTNoL219vyr0w2IN7CiSf8w3nfA5jbxAqBFQft9XeeR9GqjhAU4GuAPUztkGjRcklmudsA1zVZY3w-5S9TGkLAFJg84KdYmNqUEpv2OebOS5-XqIbitalkIp-isWUaJjdLuxDLCLl29mNnoqpL8LYDwuN967Ib0ui9Iqd9G5I9Pp4nrFf377-vLgsr398v7r4cl16KfVckjI9584jtgi15lijENRKTbo3shO8Fm2ntBJNb0wrveamk7J1WknDdQbO2IdD7m2c_i6UZrsLydMwuJGmJVkta6kUN-ZpUtTQSF7zTL7_L8kR85wEZPDdI3A7LXHM_VpUaJo8V7nGyQPl45RSpN7exrBz8c4i2FWa3dqjNLtKs6Btlpbr3h7Tl3ZH3UPV0VIGzg8A5QHvA0WbfKBspAuR_Gy7KTz5xadHCX4IY_Bu-EN3lB66sYlbsDfr5qyLAw0g8KYR_wBRlr25</recordid><startdate>20091023</startdate><enddate>20091023</enddate><creator>Collins, P.J</creator><creator>Haire, L.F</creator><creator>Lin, Y.P</creator><creator>Liu, J</creator><creator>Russell, R.J</creator><creator>Walker, P.A</creator><creator>Martin, S.R</creator><creator>Daniels, R.S</creator><creator>Gregory, V</creator><creator>Skehel, J.J</creator><creator>Gamblin, S.J</creator><creator>Hay, A.J</creator><general>Elsevier Ltd</general><general>Elsevier Limited</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>3V.</scope><scope>7QL</scope><scope>7RV</scope><scope>7T2</scope><scope>7T5</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88C</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9-</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0R</scope><scope>M0S</scope><scope>M0T</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20091023</creationdate><title>Structural basis for oseltamivir resistance of influenza viruses</title><author>Collins, P.J ; Haire, L.F ; Lin, Y.P ; Liu, J ; Russell, R.J ; Walker, P.A ; Martin, S.R ; Daniels, R.S ; Gregory, V ; Skehel, J.J ; Gamblin, S.J ; Hay, A.J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c557t-e68f22ac11b1047214133eb57e7f85d3243bd67639f88b5c728d55ba7658275d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Allergy and Immunology</topic><topic>Avian flu</topic><topic>Crystal structure</topic><topic>Drug resistance</topic><topic>Drug Resistance, Viral</topic><topic>Drugs</topic><topic>Enzymes</topic><topic>Exo-a-sialidase</topic><topic>H275Y mutation</topic><topic>Influenza A</topic><topic>Influenza A Virus, H1N1 Subtype - 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Resistance to the drug has occurred infrequently among different viruses in response to drug treatment, including A H5N1 viruses, but most notably has emerged among recently circulating A H1N1 viruses and has spread throughout the population in the absence of drug use. Crystal structures of enzyme–drug complexes, together with enzymatic properties, of mutants of H5N1 neuraminidase have provided explanations for high level oseltamivir resistance due to the common H275Y mutation, with retention of zanamivir susceptibility, and intermediate level resistance due to the N295S mutation. Complementation of enhanced NA activity due to a D344N mutation by the H275Y mutation suggests an explanation for the recent emergence and predominance of oseltamivir-resistant influenza A H1N1 viruses.</abstract><cop>Netherlands</cop><pub>Elsevier Ltd</pub><pmid>19840667</pmid><doi>10.1016/j.vaccine.2009.07.017</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Allergy and Immunology Avian flu Crystal structure Drug resistance Drug Resistance, Viral Drugs Enzymes Exo-a-sialidase H275Y mutation Influenza A Influenza A Virus, H1N1 Subtype - drug effects Influenza A Virus, H1N1 Subtype - genetics Influenza A Virus, H5N1 Subtype - drug effects Influenza A Virus, H5N1 Subtype - genetics Influenza H5N1 Models, Molecular Mutation Neuraminidase - genetics Oseltamivir Oseltamivir - chemistry Oseltamivir - pharmacology Oseltamivir resistance Protein Structure, Tertiary Studies Swine flu Viral Proteins - genetics Viruses Zanamivir |
| title | Structural basis for oseltamivir resistance of influenza viruses |
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