Molecular distribution of amino acid substitutions on neuraminidase from the 2009 (H1N1) human influenza pandemic virus.
Identifieur interne : 000973 ( PubMed/Corpus ); précédent : 000972; suivant : 000974Molecular distribution of amino acid substitutions on neuraminidase from the 2009 (H1N1) human influenza pandemic virus.
Auteurs : Miguelmiguel Quiliano ; Hugo Valdivia-Olarte ; Carlos Olivares ; David Requena ; Andrés H. Gutiérrez ; Paola Reyes-Loyola ; Luis E. Tolentino-Lopez ; Patricia Sheen ; Ver Nica Briz ; Maria A. Mu Oz-Fernández ; José Correa-Basurto ; Mirko ZimicSource :
- Bioinformation [ 0973-2063 ] ; 2013.
Abstract
The pandemic influenza AH1N1 (2009) caused an outbreak of human infection that spread to the world. Neuraminidase (NA) is an antigenic surface glycoprotein, which is essential to the influenza infection process, and is the target of anti-flu drugs oseltamivir and zanamivir. Currently, NA inhibitors are the pillar pharmacological strategy against seasonal and global influenza. Although mutations observed after NA-inhibitor treatment are characterized by changes in conserved amino acids of the enzyme catalytic site, it is possible that specific amino acid substitutions (AASs) distant from the active site such as H274Y, could confer oseltamivir or zanamivir resistance. To better understand the molecular distribution pattern of NA AASs, we analyzed NA AASs from all available reported pandemic AH1N1 NA sequences, including those reported from America, Africa, Asia, Europe, Oceania, and specifically from Mexico. The molecular distributions of the AASs were obtained at the secondary structure domain level for both the active and catalytic sites, and compared between geographic regions. Our results showed that NA AASs from America, Asia, Europe, Oceania and Mexico followed similar molecular distribution patterns. The compiled data of this study showed that highly conserved amino acids from the NA active site and catalytic site are indeed being affected by mutations. The reported NA AASs follow a similar molecular distribution pattern worldwide. Although most AASs are distributed distantly from the active site, this study shows the emergence of mutations affecting the previously conserved active and catalytic site. A significant number of unique AASs were reported simultaneously on different continents.
DOI: 10.6026/97320630009673
PubMed: 23930018
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Lima, Peru ; Drug R&D Unit, Center for Applied Pharmacobiology Research, University of Navarra, C/ Irunlarrea s/n, 31008, Pamplona, Spain.</nlm:affiliation></affiliation></author><author><name sortKey="Valdivia Olarte, Hugo" sort="Valdivia Olarte, Hugo" uniqKey="Valdivia Olarte H" first="Hugo" last="Valdivia-Olarte">Hugo Valdivia-Olarte</name></author><author><name sortKey="Olivares, Carlos" sort="Olivares, Carlos" uniqKey="Olivares C" first="Carlos" last="Olivares">Carlos Olivares</name></author><author><name sortKey="Requena, David" sort="Requena, David" uniqKey="Requena D" first="David" last="Requena">David Requena</name></author><author><name sortKey="Gutierrez, Andres H" sort="Gutierrez, Andres H" uniqKey="Gutierrez A" first="Andrés H" last="Gutiérrez">Andrés H. Gutiérrez</name></author><author><name sortKey="Reyes Loyola, Paola" sort="Reyes Loyola, Paola" uniqKey="Reyes Loyola P" first="Paola" last="Reyes-Loyola">Paola Reyes-Loyola</name></author><author><name sortKey="Tolentino Lopez, Luis E" sort="Tolentino Lopez, Luis E" uniqKey="Tolentino Lopez L" first="Luis E" last="Tolentino-Lopez">Luis E. Tolentino-Lopez</name></author><author><name sortKey="Sheen, Patricia" sort="Sheen, Patricia" uniqKey="Sheen P" first="Patricia" last="Sheen">Patricia Sheen</name></author><author><name sortKey="Briz, Ver Nica" sort="Briz, Ver Nica" uniqKey="Briz V" first="Ver Nica" last="Briz">Ver Nica Briz</name></author><author><name sortKey="Mu Oz Fernandez, Maria A" sort="Mu Oz Fernandez, Maria A" uniqKey="Mu Oz Fernandez M" first="Maria A" last="Mu Oz-Fernández">Maria A. Mu Oz-Fernández</name></author><author><name sortKey="Correa Basurto, Jose" sort="Correa Basurto, Jose" uniqKey="Correa Basurto J" first="José" last="Correa-Basurto">José Correa-Basurto</name></author><author><name sortKey="Zimic, Mirko" sort="Zimic, Mirko" uniqKey="Zimic M" first="Mirko" last="Zimic">Mirko Zimic</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23930018</idno><idno type="pmid">23930018</idno><idno type="doi">10.6026/97320630009673</idno><idno type="wicri:Area/PubMed/Corpus">000973</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000973</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Molecular distribution of amino acid substitutions on neuraminidase from the 2009 (H1N1) human influenza pandemic virus.</title><author><name sortKey="Quiliano, Miguelmiguel" sort="Quiliano, Miguelmiguel" uniqKey="Quiliano M" first="Miguelmiguel" last="Quiliano">Miguelmiguel Quiliano</name><affiliation><nlm:affiliation>Laboratorio de Bioinformática y Biología Molecular, Laboratorios de Investigación y Desarrollo, Facultad de Ciencias y Filosofía, Universidad Peruana Cayetano Heredia. Av. Honorio Delgado, 430. SMP. Lima, Peru ; Drug R&D Unit, Center for Applied Pharmacobiology Research, University of Navarra, C/ Irunlarrea s/n, 31008, Pamplona, Spain.</nlm:affiliation></affiliation></author><author><name sortKey="Valdivia Olarte, Hugo" sort="Valdivia Olarte, Hugo" uniqKey="Valdivia Olarte H" first="Hugo" last="Valdivia-Olarte">Hugo Valdivia-Olarte</name></author><author><name sortKey="Olivares, Carlos" sort="Olivares, Carlos" uniqKey="Olivares C" first="Carlos" last="Olivares">Carlos Olivares</name></author><author><name sortKey="Requena, David" sort="Requena, David" uniqKey="Requena D" first="David" last="Requena">David Requena</name></author><author><name sortKey="Gutierrez, Andres H" sort="Gutierrez, Andres H" uniqKey="Gutierrez A" first="Andrés H" last="Gutiérrez">Andrés H. Gutiérrez</name></author><author><name sortKey="Reyes Loyola, Paola" sort="Reyes Loyola, Paola" uniqKey="Reyes Loyola P" first="Paola" last="Reyes-Loyola">Paola Reyes-Loyola</name></author><author><name sortKey="Tolentino Lopez, Luis E" sort="Tolentino Lopez, Luis E" uniqKey="Tolentino Lopez L" first="Luis E" last="Tolentino-Lopez">Luis E. Tolentino-Lopez</name></author><author><name sortKey="Sheen, Patricia" sort="Sheen, Patricia" uniqKey="Sheen P" first="Patricia" last="Sheen">Patricia Sheen</name></author><author><name sortKey="Briz, Ver Nica" sort="Briz, Ver Nica" uniqKey="Briz V" first="Ver Nica" last="Briz">Ver Nica Briz</name></author><author><name sortKey="Mu Oz Fernandez, Maria A" sort="Mu Oz Fernandez, Maria A" uniqKey="Mu Oz Fernandez M" first="Maria A" last="Mu Oz-Fernández">Maria A. Mu Oz-Fernández</name></author><author><name sortKey="Correa Basurto, Jose" sort="Correa Basurto, Jose" uniqKey="Correa Basurto J" first="José" last="Correa-Basurto">José Correa-Basurto</name></author><author><name sortKey="Zimic, Mirko" sort="Zimic, Mirko" uniqKey="Zimic M" first="Mirko" last="Zimic">Mirko Zimic</name></author></analytic><series><title level="j">Bioinformation</title><idno type="ISSN">0973-2063</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The pandemic influenza AH1N1 (2009) caused an outbreak of human infection that spread to the world. Neuraminidase (NA) is an antigenic surface glycoprotein, which is essential to the influenza infection process, and is the target of anti-flu drugs oseltamivir and zanamivir. Currently, NA inhibitors are the pillar pharmacological strategy against seasonal and global influenza. Although mutations observed after NA-inhibitor treatment are characterized by changes in conserved amino acids of the enzyme catalytic site, it is possible that specific amino acid substitutions (AASs) distant from the active site such as H274Y, could confer oseltamivir or zanamivir resistance. To better understand the molecular distribution pattern of NA AASs, we analyzed NA AASs from all available reported pandemic AH1N1 NA sequences, including those reported from America, Africa, Asia, Europe, Oceania, and specifically from Mexico. The molecular distributions of the AASs were obtained at the secondary structure domain level for both the active and catalytic sites, and compared between geographic regions. Our results showed that NA AASs from America, Asia, Europe, Oceania and Mexico followed similar molecular distribution patterns. The compiled data of this study showed that highly conserved amino acids from the NA active site and catalytic site are indeed being affected by mutations. The reported NA AASs follow a similar molecular distribution pattern worldwide. Although most AASs are distributed distantly from the active site, this study shows the emergence of mutations affecting the previously conserved active and catalytic site. A significant number of unique AASs were reported simultaneously on different continents. </div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">23930018</PMID><DateCompleted><Year>2013</Year><Month>08</Month><Day>09</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>06</Day></DateRevised><Article PubModel="Electronic-Print"><Journal><ISSN IssnType="Print">0973-2063</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>13</Issue><PubDate><Year>2013</Year></PubDate></JournalIssue><Title>Bioinformation</Title><ISOAbbreviation>Bioinformation</ISOAbbreviation></Journal><ArticleTitle>Molecular distribution of amino acid substitutions on neuraminidase from the 2009 (H1N1) human influenza pandemic virus.</ArticleTitle><Pagination><MedlinePgn>673-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.6026/97320630009673</ELocationID><Abstract><AbstractText>The pandemic influenza AH1N1 (2009) caused an outbreak of human infection that spread to the world. Neuraminidase (NA) is an antigenic surface glycoprotein, which is essential to the influenza infection process, and is the target of anti-flu drugs oseltamivir and zanamivir. Currently, NA inhibitors are the pillar pharmacological strategy against seasonal and global influenza. Although mutations observed after NA-inhibitor treatment are characterized by changes in conserved amino acids of the enzyme catalytic site, it is possible that specific amino acid substitutions (AASs) distant from the active site such as H274Y, could confer oseltamivir or zanamivir resistance. To better understand the molecular distribution pattern of NA AASs, we analyzed NA AASs from all available reported pandemic AH1N1 NA sequences, including those reported from America, Africa, Asia, Europe, Oceania, and specifically from Mexico. The molecular distributions of the AASs were obtained at the secondary structure domain level for both the active and catalytic sites, and compared between geographic regions. Our results showed that NA AASs from America, Asia, Europe, Oceania and Mexico followed similar molecular distribution patterns. The compiled data of this study showed that highly conserved amino acids from the NA active site and catalytic site are indeed being affected by mutations. The reported NA AASs follow a similar molecular distribution pattern worldwide. Although most AASs are distributed distantly from the active site, this study shows the emergence of mutations affecting the previously conserved active and catalytic site. A significant number of unique AASs were reported simultaneously on different continents. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Quiliano</LastName><ForeName>Miguelmiguel</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratorio de Bioinformática y Biología Molecular, Laboratorios de Investigación y Desarrollo, Facultad de Ciencias y Filosofía, Universidad Peruana Cayetano Heredia. Av. Honorio Delgado, 430. SMP. Lima, Peru ; Drug R&D Unit, Center for Applied Pharmacobiology Research, University of Navarra, C/ Irunlarrea s/n, 31008, Pamplona, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Valdivia-Olarte</LastName><ForeName>Hugo</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Olivares</LastName><ForeName>Carlos</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Requena</LastName><ForeName>David</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Gutiérrez</LastName><ForeName>Andrés H</ForeName><Initials>AH</Initials></Author><Author ValidYN="Y"><LastName>Reyes-Loyola</LastName><ForeName>Paola</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Tolentino-Lopez</LastName><ForeName>Luis E</ForeName><Initials>LE</Initials></Author><Author ValidYN="Y"><LastName>Sheen</LastName><ForeName>Patricia</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Briz</LastName><ForeName>Verónica</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Muñoz-Fernández</LastName><ForeName>Maria A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Correa-Basurto</LastName><ForeName>José</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Zimic</LastName><ForeName>Mirko</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>07</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>Singapore</Country><MedlineTA>Bioinformation</MedlineTA><NlmUniqueID>101258255</NlmUniqueID><ISSNLinking>0973-2063</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Geographic regions</Keyword><Keyword MajorTopicYN="N">Influenza</Keyword><Keyword MajorTopicYN="N">Molecular distribution pattern</Keyword><Keyword MajorTopicYN="N">Neuraminidase</Keyword><Keyword MajorTopicYN="N">Pandemic H1N1 (2009)</Keyword><Keyword MajorTopicYN="N">amino acid substitution</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>05</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>05</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>8</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>8</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>8</Month><Day>10</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23930018</ArticleId><ArticleId 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