Neuraminidase inhibitor susceptibility of porcine H3N2 influenza A viruses isolated in Germany between 1982 and 1999.
Identifieur interne : 000471 ( Main/Exploration ); précédent : 000470; suivant : 000472Neuraminidase inhibitor susceptibility of porcine H3N2 influenza A viruses isolated in Germany between 1982 and 1999.
Auteurs : Katja Bauer [Allemagne] ; Christina Schrader ; Jochen Suess ; Peter Wutzler ; Michaela SchmidtkeSource :
- Antiviral research [ 0166-3542 ] ; 2007.
Descripteurs français
- KwdFr :
- Allemagne (MeSH), Amantadine (pharmacologie), Animaux (MeSH), Antienzymes (pharmacologie), Antiviraux (pharmacologie), Glycoprotéine hémagglutinine du virus influenza (composition chimique), Hémagglutination virale (MeSH), Lignée cellulaire (MeSH), Oséltamivir (pharmacologie), Résistance virale aux médicaments (MeSH), Sialidase (antagonistes et inhibiteurs), Sialidase (composition chimique), Sialidase (métabolisme), Sous-type H3N2 du virus de la grippe A (effets des médicaments et des substances chimiques), Sous-type H3N2 du virus de la grippe A (isolement et purification), Sous-type H3N2 du virus de la grippe A (métabolisme), Substitution d'acide aminé (MeSH), Suidae (MeSH), Zanamivir (pharmacologie).
- MESH :
- antagonistes et inhibiteurs : Sialidase.
- composition chimique : Glycoprotéine hémagglutinine du virus influenza, Sialidase.
- effets des médicaments et des substances chimiques : Sous-type H3N2 du virus de la grippe A.
- isolement et purification : Sous-type H3N2 du virus de la grippe A.
- métabolisme : Sialidase, Sous-type H3N2 du virus de la grippe A.
- pharmacologie : Amantadine, Antienzymes, Antiviraux, Oséltamivir, Zanamivir.
- Allemagne, Animaux, Hémagglutination virale, Lignée cellulaire, Résistance virale aux médicaments, Substitution d'acide aminé, Suidae.
- Wicri :
- geographic : Allemagne.
English descriptors
- KwdEn :
- Amantadine (pharmacology), Amino Acid Substitution (MeSH), Animals (MeSH), Antiviral Agents (pharmacology), Cell Line (MeSH), Drug Resistance, Viral (MeSH), Enzyme Inhibitors (pharmacology), Germany (MeSH), Hemagglutination, Viral (MeSH), Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Influenza A Virus, H3N2 Subtype (drug effects), Influenza A Virus, H3N2 Subtype (isolation & purification), Influenza A Virus, H3N2 Subtype (metabolism), Neuraminidase (antagonists & inhibitors), Neuraminidase (chemistry), Neuraminidase (metabolism), Oseltamivir (pharmacology), Swine (MeSH), Zanamivir (pharmacology).
- MESH :
- chemical , antagonists & inhibitors : Neuraminidase.
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus, Neuraminidase.
- chemical , metabolism : Neuraminidase.
- chemical , pharmacology : Amantadine, Antiviral Agents, Enzyme Inhibitors, Oseltamivir, Zanamivir.
- geographic : Germany.
- drug effects : Influenza A Virus, H3N2 Subtype.
- isolation & purification : Influenza A Virus, H3N2 Subtype.
- metabolism : Influenza A Virus, H3N2 Subtype.
- Amino Acid Substitution, Animals, Cell Line, Drug Resistance, Viral, Hemagglutination, Viral, Swine.
Abstract
As an intermediate host of avian and human influenza A viruses (FLUAV) pigs may play a potential role in interspecies virus transmission and reassortment of viral genes including those conferring antiviral drug resistance. Porcine FLUAV isolated in Germany between 1989 and 2001 contains mutations in the M2 gene inducing amantadine resistance. No data exist on neuraminidase inhibitor (NAI) susceptibility of these porcine FLUAV. We studied the antiviral activity of NAI against seven selected H3N2 FLUAV isolated from pigs in Germany between 1982 and 1999. All isolates were susceptible towards oseltamivir and zanamivir in neuraminidase enzyme-inhibition assays. Both compounds inhibited virus spreading and reduced the virus yields and plaque size at low concentrations. Higher concentrations were necessary to reduce the plaque number. Two isolates that differed in glycosylation pattern of viral hemagglutinin (HA) showed markedly reduced drug susceptibility in cell culture-based assays.
DOI: 10.1016/j.antiviral.2007.03.007
PubMed: 17445913
Affiliations:
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Jena</wicri:noRegion></affiliation></author><author><name sortKey="Schrader, Christina" sort="Schrader, Christina" uniqKey="Schrader C" first="Christina" last="Schrader">Christina Schrader</name></author><author><name sortKey="Suess, Jochen" sort="Suess, Jochen" uniqKey="Suess J" first="Jochen" last="Suess">Jochen Suess</name></author><author><name sortKey="Wutzler, Peter" sort="Wutzler, Peter" uniqKey="Wutzler P" first="Peter" last="Wutzler">Peter Wutzler</name></author><author><name sortKey="Schmidtke, Michaela" sort="Schmidtke, Michaela" uniqKey="Schmidtke M" first="Michaela" last="Schmidtke">Michaela Schmidtke</name></author></analytic><series><title level="j">Antiviral research</title><idno type="ISSN">0166-3542</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amantadine (pharmacology)</term><term>Amino Acid Substitution 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hémagglutinine du virus influenza (composition chimique)</term><term>Hémagglutination virale (MeSH)</term><term>Lignée cellulaire (MeSH)</term><term>Oséltamivir (pharmacologie)</term><term>Résistance virale aux médicaments (MeSH)</term><term>Sialidase (antagonistes et inhibiteurs)</term><term>Sialidase (composition chimique)</term><term>Sialidase (métabolisme)</term><term>Sous-type H3N2 du virus de la grippe A (effets des médicaments et des substances chimiques)</term><term>Sous-type H3N2 du virus de la grippe A (isolement et purification)</term><term>Sous-type H3N2 du virus de la grippe A (métabolisme)</term><term>Substitution d'acide aminé (MeSH)</term><term>Suidae (MeSH)</term><term>Zanamivir (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Amantadine</term><term>Antiviral Agents</term><term>Enzyme Inhibitors</term><term>Oseltamivir</term><term>Zanamivir</term></keywords><keywords scheme="MESH" type="geographic" xml:lang="en"><term>Germany</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Sialidase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Sialidase</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Influenza A Virus, H3N2 Subtype</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Sous-type H3N2 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Influenza A Virus, H3N2 Subtype</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Sous-type H3N2 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza A Virus, H3N2 Subtype</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Sialidase</term><term>Sous-type H3N2 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Amantadine</term><term>Antienzymes</term><term>Antiviraux</term><term>Oséltamivir</term><term>Zanamivir</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Animals</term><term>Cell Line</term><term>Drug Resistance, Viral</term><term>Hemagglutination, Viral</term><term>Swine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Allemagne</term><term>Animaux</term><term>Hémagglutination virale</term><term>Lignée cellulaire</term><term>Résistance virale aux médicaments</term><term>Substitution d'acide aminé</term><term>Suidae</term></keywords><keywords scheme="Wicri" type="geographic" xml:lang="fr"><term>Allemagne</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">As an intermediate host of avian and human influenza A viruses (FLUAV) pigs may play a potential role in interspecies virus transmission and reassortment of viral genes including those conferring antiviral drug resistance. Porcine FLUAV isolated in Germany between 1989 and 2001 contains mutations in the M2 gene inducing amantadine resistance. No data exist on neuraminidase inhibitor (NAI) susceptibility of these porcine FLUAV. We studied the antiviral activity of NAI against seven selected H3N2 FLUAV isolated from pigs in Germany between 1982 and 1999. All isolates were susceptible towards oseltamivir and zanamivir in neuraminidase enzyme-inhibition assays. Both compounds inhibited virus spreading and reduced the virus yields and plaque size at low concentrations. Higher concentrations were necessary to reduce the plaque number. Two isolates that differed in glycosylation pattern of viral hemagglutinin (HA) showed markedly reduced drug susceptibility in cell culture-based assays.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17445913</PMID><DateCompleted><Year>2007</Year><Month>11</Month><Day>07</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0166-3542</ISSN><JournalIssue CitedMedium="Print"><Volume>75</Volume><Issue>3</Issue><PubDate><Year>2007</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Antiviral research</Title><ISOAbbreviation>Antiviral Res.</ISOAbbreviation></Journal><ArticleTitle>Neuraminidase inhibitor susceptibility of porcine H3N2 influenza A viruses isolated in Germany between 1982 and 1999.</ArticleTitle><Pagination><MedlinePgn>219-26</MedlinePgn></Pagination><Abstract><AbstractText>As an intermediate host of avian and human influenza A viruses (FLUAV) pigs may play a potential role in interspecies virus transmission and reassortment of viral genes including those conferring antiviral drug resistance. Porcine FLUAV isolated in Germany between 1989 and 2001 contains mutations in the M2 gene inducing amantadine resistance. No data exist on neuraminidase inhibitor (NAI) susceptibility of these porcine FLUAV. We studied the antiviral activity of NAI against seven selected H3N2 FLUAV isolated from pigs in Germany between 1982 and 1999. All isolates were susceptible towards oseltamivir and zanamivir in neuraminidase enzyme-inhibition assays. Both compounds inhibited virus spreading and reduced the virus yields and plaque size at low concentrations. Higher concentrations were necessary to reduce the plaque number. Two isolates that differed in glycosylation pattern of viral hemagglutinin (HA) showed markedly reduced drug susceptibility in cell culture-based assays.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bauer</LastName><ForeName>Katja</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Institute of Virology and Antiviral Therapy, Medical Centre of the Friedrich Schiller University Jena, Hans Knoell Str. 2, PF, D-07740 Jena, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schrader</LastName><ForeName>Christina</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Suess</LastName><ForeName>Jochen</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Wutzler</LastName><ForeName>Peter</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Schmidtke</LastName><ForeName>Michaela</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>04</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Antiviral Res</MedlineTA><NlmUniqueID>8109699</NlmUniqueID><ISSNLinking>0166-3542</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019267">Hemagglutinin Glycoproteins, Influenza 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MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D024882" MajorTopicYN="N">Drug Resistance, Viral</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005858" MajorTopicYN="N" Type="Geographic">Germany</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006387" MajorTopicYN="N">Hemagglutination, Viral</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019267" MajorTopicYN="N">Hemagglutinin Glycoproteins, Influenza Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053122" MajorTopicYN="N">Influenza A Virus, H3N2 Subtype</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009439" MajorTopicYN="N">Neuraminidase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053139" MajorTopicYN="N">Oseltamivir</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053243" MajorTopicYN="N">Zanamivir</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>12</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2007</Year><Month>02</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>03</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>4</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>11</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>4</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17445913</ArticleId><ArticleId IdType="pii">S0166-3542(07)00259-8</ArticleId><ArticleId IdType="doi">10.1016/j.antiviral.2007.03.007</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Schmidtke, Michaela" sort="Schmidtke, Michaela" uniqKey="Schmidtke M" first="Michaela" last="Schmidtke">Michaela Schmidtke</name><name sortKey="Schrader, Christina" sort="Schrader, Christina" uniqKey="Schrader C" first="Christina" last="Schrader">Christina Schrader</name><name sortKey="Suess, Jochen" sort="Suess, Jochen" uniqKey="Suess J" first="Jochen" last="Suess">Jochen Suess</name><name sortKey="Wutzler, Peter" sort="Wutzler, Peter" uniqKey="Wutzler P" first="Peter" last="Wutzler">Peter Wutzler</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Bauer, Katja" sort="Bauer, Katja" uniqKey="Bauer K" first="Katja" last="Bauer">Katja Bauer</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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