Neuraminidase inhibitor susceptibility and neuraminidase enzyme kinetics of human influenza A and B viruses circulating in Thailand in 2010-2015
Amino acid substitutions within or near the active site of the viral neuraminidase (NA) may affect influenza virus fitness. In influenza A(H3N2) and B viruses circulating in Thailand between 2010 and 2015, we identified several NA substitutions that were previously reported to be associated with red...
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| description | Amino acid substitutions within or near the active site of the viral neuraminidase (NA) may affect influenza virus fitness. In influenza A(H3N2) and B viruses circulating in Thailand between 2010 and 2015, we identified several NA substitutions that were previously reported to be associated with reduced inhibition by NA inhibitors (NAIs). To study the effect of these substitutions on the enzymatic properties of NA and on virus characteristics, we generated recombinant influenza viruses possessing either a wild type (WT) NA or an NA with a single I222V, S331G, or S331R substitution [in influenza A(H3N2) viruses] or a single D342S, A395T, A395V, or A395D NA substitution (in influenza B viruses). We generated recombinant (7:1) influenza A and B viruses on the genetic background of A/Puerto Rico/8/1934 (A/PR/8, H1N1) or B/Yamanashi/166/1998 (B/YAM) viruses, respectively. In contrast to the expected phenotypes, all the recombinant influenza A(H3N2) and B viruses carrying putative NA resistance substitutions were susceptible to NAIs. The Km and Vmax for the NAs of A/PR8-S331G and A/PR8-S331R viruses were higher than for the NA of WT virus, and the corresponding values for the B/YAM-D342S virus were lower than for the NA of WT virus. Although there was initial variation in the kinetics of influenza A and B viruses' replication in MDCK cells, their titers were comparable to each other and to WT viruses at later time points. All introduced substitutions were stable except for B/YAM-D342S and B/YAM-A395V which reverted to WT sequences after three passages. Our data suggest that inferring susceptibility to NAIs based on sequence information alone should be cautioned. The impact of NA substitution on NAI resistance, viral growth, and enzymatic properties is viral context dependent and should be empirically determined. |
| doi_str_mv | 10.1371/journal.pone.0190877 |
| format | Article |
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In influenza A(H3N2) and B viruses circulating in Thailand between 2010 and 2015, we identified several NA substitutions that were previously reported to be associated with reduced inhibition by NA inhibitors (NAIs). To study the effect of these substitutions on the enzymatic properties of NA and on virus characteristics, we generated recombinant influenza viruses possessing either a wild type (WT) NA or an NA with a single I222V, S331G, or S331R substitution [in influenza A(H3N2) viruses] or a single D342S, A395T, A395V, or A395D NA substitution (in influenza B viruses). We generated recombinant (7:1) influenza A and B viruses on the genetic background of A/Puerto Rico/8/1934 (A/PR/8, H1N1) or B/Yamanashi/166/1998 (B/YAM) viruses, respectively. In contrast to the expected phenotypes, all the recombinant influenza A(H3N2) and B viruses carrying putative NA resistance substitutions were susceptible to NAIs. The Km and Vmax for the NAs of A/PR8-S331G and A/PR8-S331R viruses were higher than for the NA of WT virus, and the corresponding values for the B/YAM-D342S virus were lower than for the NA of WT virus. Although there was initial variation in the kinetics of influenza A and B viruses' replication in MDCK cells, their titers were comparable to each other and to WT viruses at later time points. All introduced substitutions were stable except for B/YAM-D342S and B/YAM-A395V which reverted to WT sequences after three passages. Our data suggest that inferring susceptibility to NAIs based on sequence information alone should be cautioned. The impact of NA substitution on NAI resistance, viral growth, and enzymatic properties is viral context dependent and should be empirically determined.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0190877</identifier><identifier>PMID: 29324781</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Substitution ; Amino acids ; Animals ; Antiviral Agents - pharmacology ; Avian flu ; Betainfluenzavirus - drug effects ; Betainfluenzavirus - enzymology ; Betainfluenzavirus - genetics ; Betainfluenzavirus - physiology ; Biology and life sciences ; Dogs ; Drug Resistance, Viral - genetics ; Enzyme Inhibitors - pharmacology ; Enzyme Stability - genetics ; Enzymes ; Exo-a-sialidase ; FDA approval ; Fitness ; Genomic Instability ; Humans ; Infectious diseases ; Influenza ; Influenza A ; Influenza A virus - drug effects ; Influenza A virus - enzymology ; Influenza A virus - genetics ; Influenza A virus - physiology ; Influenza A Virus, H1N1 Subtype - drug effects ; Influenza A Virus, H1N1 Subtype - enzymology ; Influenza A Virus, H1N1 Subtype - genetics ; Influenza A Virus, H1N1 Subtype - physiology ; Influenza A Virus, H3N2 Subtype - drug effects ; Influenza A Virus, H3N2 Subtype - enzymology ; Influenza A Virus, H3N2 Subtype - genetics ; Influenza A Virus, H3N2 Subtype - physiology ; Influenza B ; Influenza viruses ; Influenza, Human - virology ; Kinetics ; Madin Darby Canine Kidney Cells ; Medicine ; Medicine and health sciences ; Mutation ; Neuraminidase - antagonists & inhibitors ; Neuraminidase - genetics ; Neuraminidase - metabolism ; Pediatrics ; Physical Sciences ; Plasmids ; Reproductive fitness ; Substitutes ; Surveillance ; Thailand ; Viral Proteins - antagonists & inhibitors ; Viral Proteins - genetics ; Viral Proteins - metabolism ; Virology ; Virus replication ; Virus Replication - drug effects ; Virus Replication - genetics ; Virus Replication - physiology ; Viruses</subject><ispartof>PloS one, 2018-01, Vol.13 (1), p.e0190877</ispartof><rights>COPYRIGHT 2018 Public Library of Science</rights><rights>2018 Tewawong et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2018 Tewawong et al 2018 Tewawong et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-1ee34139aeeeb312ee99794f678d99f7241787bfdaa85fc64eb60296e21acae83</citedby><cites>FETCH-LOGICAL-c758t-1ee34139aeeeb312ee99794f678d99f7241787bfdaa85fc64eb60296e21acae83</cites><orcidid>0000-0001-9067-5682</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5764337/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5764337/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29324781$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Tompkins, Stephen Mark</contributor><creatorcontrib>Tewawong, Nipaporn</creatorcontrib><creatorcontrib>Marathe, Bindumadhav M</creatorcontrib><creatorcontrib>Poovorawan, Yong</creatorcontrib><creatorcontrib>Vongpunsawad, Sompong</creatorcontrib><creatorcontrib>Webby, Richard J</creatorcontrib><creatorcontrib>Govorkova, Elena A</creatorcontrib><title>Neuraminidase inhibitor susceptibility and neuraminidase enzyme kinetics of human influenza A and B viruses circulating in Thailand in 2010-2015</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Amino acid substitutions within or near the active site of the viral neuraminidase (NA) may affect influenza virus fitness. In influenza A(H3N2) and B viruses circulating in Thailand between 2010 and 2015, we identified several NA substitutions that were previously reported to be associated with reduced inhibition by NA inhibitors (NAIs). To study the effect of these substitutions on the enzymatic properties of NA and on virus characteristics, we generated recombinant influenza viruses possessing either a wild type (WT) NA or an NA with a single I222V, S331G, or S331R substitution [in influenza A(H3N2) viruses] or a single D342S, A395T, A395V, or A395D NA substitution (in influenza B viruses). We generated recombinant (7:1) influenza A and B viruses on the genetic background of A/Puerto Rico/8/1934 (A/PR/8, H1N1) or B/Yamanashi/166/1998 (B/YAM) viruses, respectively. In contrast to the expected phenotypes, all the recombinant influenza A(H3N2) and B viruses carrying putative NA resistance substitutions were susceptible to NAIs. The Km and Vmax for the NAs of A/PR8-S331G and A/PR8-S331R viruses were higher than for the NA of WT virus, and the corresponding values for the B/YAM-D342S virus were lower than for the NA of WT virus. Although there was initial variation in the kinetics of influenza A and B viruses' replication in MDCK cells, their titers were comparable to each other and to WT viruses at later time points. All introduced substitutions were stable except for B/YAM-D342S and B/YAM-A395V which reverted to WT sequences after three passages. Our data suggest that inferring susceptibility to NAIs based on sequence information alone should be cautioned. The impact of NA substitution on NAI resistance, viral growth, and enzymatic properties is viral context dependent and should be empirically determined.</description><subject>Amino Acid Substitution</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antiviral Agents - pharmacology</subject><subject>Avian flu</subject><subject>Betainfluenzavirus - drug effects</subject><subject>Betainfluenzavirus - enzymology</subject><subject>Betainfluenzavirus - genetics</subject><subject>Betainfluenzavirus - physiology</subject><subject>Biology and life sciences</subject><subject>Dogs</subject><subject>Drug Resistance, Viral - genetics</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzyme Stability - genetics</subject><subject>Enzymes</subject><subject>Exo-a-sialidase</subject><subject>FDA approval</subject><subject>Fitness</subject><subject>Genomic Instability</subject><subject>Humans</subject><subject>Infectious diseases</subject><subject>Influenza</subject><subject>Influenza A</subject><subject>Influenza A virus - drug effects</subject><subject>Influenza A virus - enzymology</subject><subject>Influenza A virus - genetics</subject><subject>Influenza A virus - physiology</subject><subject>Influenza A Virus, H1N1 Subtype - drug effects</subject><subject>Influenza A Virus, H1N1 Subtype - enzymology</subject><subject>Influenza A Virus, H1N1 Subtype - genetics</subject><subject>Influenza A Virus, H1N1 Subtype - physiology</subject><subject>Influenza A Virus, H3N2 Subtype - drug effects</subject><subject>Influenza A Virus, H3N2 Subtype - enzymology</subject><subject>Influenza A Virus, H3N2 Subtype - genetics</subject><subject>Influenza A Virus, H3N2 Subtype - physiology</subject><subject>Influenza B</subject><subject>Influenza viruses</subject><subject>Influenza, Human - virology</subject><subject>Kinetics</subject><subject>Madin Darby Canine Kidney Cells</subject><subject>Medicine</subject><subject>Medicine and health sciences</subject><subject>Mutation</subject><subject>Neuraminidase - antagonists & inhibitors</subject><subject>Neuraminidase - genetics</subject><subject>Neuraminidase - metabolism</subject><subject>Pediatrics</subject><subject>Physical Sciences</subject><subject>Plasmids</subject><subject>Reproductive fitness</subject><subject>Substitutes</subject><subject>Surveillance</subject><subject>Thailand</subject><subject>Viral Proteins - antagonists & inhibitors</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><subject>Virology</subject><subject>Virus replication</subject><subject>Virus Replication - drug effects</subject><subject>Virus Replication - genetics</subject><subject>Virus Replication - physiology</subject><subject>Viruses</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNk9-K1DAUxoso7rr6BqIFQfBixiZpm_ZGGBf_DCwu6OptOJOeTDO2yZiki-NT-MhmdrrLFBSk0KY5v-9L-jUnSZ6SbE4YJ683dnAGuvnWGpxnpM4qzu8lp6RmdFbSjN0_Gp8kj7zfZFnBqrJ8mJzQWMh5RU6T359wcNBroxvwmGrT6pUO1qV-8BK3Ib51OuxSME1qJiiaX7se0-_aYNDSp1al7dCDiR6qG2IV0sWN7G16rd3g0adSOzl0ELRZRyq9akF3eyKOaUayWbwVj5MHCjqPT8bnWfL1_bur84-zi8sPy_PFxUzyogozgshywmpAxBUjFLGueZ2rkldNXStOc8IrvlINQFUoWea4KjNal0gJSMCKnSXPD77bznoxhukFqWNCnBblnlgeiMbCRmyd7sHthAUtbiasWwtw8dM7FLKMlgqANqDyhqkqk1DkDZU5yJyVq-j1ZlxtWPXYSDTBQTcxnVaMbsXaXouClzljPBq8GA2c_TGgD__Y8kitIe4q_ggbzWSvvRSLgtKCMFqRSM3_QsWrwV7LeJyUjvMTwauJIDIBf4Y1DN6L5ZfP_89efpuyL4_YFqELrbfdELQ1fgrmB1A6671DdZccycS-G27TEPtuEGM3RNmz49TvRLfHn_0BApQHkw</recordid><startdate>20180111</startdate><enddate>20180111</enddate><creator>Tewawong, Nipaporn</creator><creator>Marathe, Bindumadhav M</creator><creator>Poovorawan, Yong</creator><creator>Vongpunsawad, Sompong</creator><creator>Webby, Richard J</creator><creator>Govorkova, Elena A</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0001-9067-5682</orcidid></search><sort><creationdate>20180111</creationdate><title>Neuraminidase inhibitor susceptibility and neuraminidase enzyme kinetics of human influenza A and B viruses circulating in Thailand in 2010-2015</title><author>Tewawong, Nipaporn ; Marathe, Bindumadhav M ; Poovorawan, Yong ; Vongpunsawad, Sompong ; Webby, Richard J ; Govorkova, Elena A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c758t-1ee34139aeeeb312ee99794f678d99f7241787bfdaa85fc64eb60296e21acae83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Amino Acid Substitution</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Antiviral Agents - 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Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tewawong, Nipaporn</au><au>Marathe, Bindumadhav M</au><au>Poovorawan, Yong</au><au>Vongpunsawad, Sompong</au><au>Webby, Richard J</au><au>Govorkova, Elena A</au><au>Tompkins, Stephen Mark</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Neuraminidase inhibitor susceptibility and neuraminidase enzyme kinetics of human influenza A and B viruses circulating in Thailand in 2010-2015</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2018-01-11</date><risdate>2018</risdate><volume>13</volume><issue>1</issue><spage>e0190877</spage><pages>e0190877-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Amino acid substitutions within or near the active site of the viral neuraminidase (NA) may affect influenza virus fitness. In influenza A(H3N2) and B viruses circulating in Thailand between 2010 and 2015, we identified several NA substitutions that were previously reported to be associated with reduced inhibition by NA inhibitors (NAIs). To study the effect of these substitutions on the enzymatic properties of NA and on virus characteristics, we generated recombinant influenza viruses possessing either a wild type (WT) NA or an NA with a single I222V, S331G, or S331R substitution [in influenza A(H3N2) viruses] or a single D342S, A395T, A395V, or A395D NA substitution (in influenza B viruses). We generated recombinant (7:1) influenza A and B viruses on the genetic background of A/Puerto Rico/8/1934 (A/PR/8, H1N1) or B/Yamanashi/166/1998 (B/YAM) viruses, respectively. In contrast to the expected phenotypes, all the recombinant influenza A(H3N2) and B viruses carrying putative NA resistance substitutions were susceptible to NAIs. The Km and Vmax for the NAs of A/PR8-S331G and A/PR8-S331R viruses were higher than for the NA of WT virus, and the corresponding values for the B/YAM-D342S virus were lower than for the NA of WT virus. Although there was initial variation in the kinetics of influenza A and B viruses' replication in MDCK cells, their titers were comparable to each other and to WT viruses at later time points. All introduced substitutions were stable except for B/YAM-D342S and B/YAM-A395V which reverted to WT sequences after three passages. Our data suggest that inferring susceptibility to NAIs based on sequence information alone should be cautioned. The impact of NA substitution on NAI resistance, viral growth, and enzymatic properties is viral context dependent and should be empirically determined.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>29324781</pmid><doi>10.1371/journal.pone.0190877</doi><tpages>e0190877</tpages><orcidid>https://orcid.org/0000-0001-9067-5682</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2018-01, Vol.13 (1), p.e0190877 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1986672568 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry; Public Library of Science (PLoS) |
| subjects | Amino Acid Substitution Amino acids Animals Antiviral Agents - pharmacology Avian flu Betainfluenzavirus - drug effects Betainfluenzavirus - enzymology Betainfluenzavirus - genetics Betainfluenzavirus - physiology Biology and life sciences Dogs Drug Resistance, Viral - genetics Enzyme Inhibitors - pharmacology Enzyme Stability - genetics Enzymes Exo-a-sialidase FDA approval Fitness Genomic Instability Humans Infectious diseases Influenza Influenza A Influenza A virus - drug effects Influenza A virus - enzymology Influenza A virus - genetics Influenza A virus - physiology Influenza A Virus, H1N1 Subtype - drug effects Influenza A Virus, H1N1 Subtype - enzymology Influenza A Virus, H1N1 Subtype - genetics Influenza A Virus, H1N1 Subtype - physiology Influenza A Virus, H3N2 Subtype - drug effects Influenza A Virus, H3N2 Subtype - enzymology Influenza A Virus, H3N2 Subtype - genetics Influenza A Virus, H3N2 Subtype - physiology Influenza B Influenza viruses Influenza, Human - virology Kinetics Madin Darby Canine Kidney Cells Medicine Medicine and health sciences Mutation Neuraminidase - antagonists & inhibitors Neuraminidase - genetics Neuraminidase - metabolism Pediatrics Physical Sciences Plasmids Reproductive fitness Substitutes Surveillance Thailand Viral Proteins - antagonists & inhibitors Viral Proteins - genetics Viral Proteins - metabolism Virology Virus replication Virus Replication - drug effects Virus Replication - genetics Virus Replication - physiology Viruses |
| title | Neuraminidase inhibitor susceptibility and neuraminidase enzyme kinetics of human influenza A and B viruses circulating in Thailand in 2010-2015 |
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