Effects of single-point amino acid substitutions on the structure and function neuraminidase proteins in influenza A virus.
Identifieur interne : 000261 ( PubMed/Curation ); précédent : 000260; suivant : 000262Effects of single-point amino acid substitutions on the structure and function neuraminidase proteins in influenza A virus.
Auteurs : Takuya Yano [Japon] ; Eri Nobusawa ; Alexander Nagy ; Setsuko Nakajima ; Katsuhisa NakajimaSource :
- Microbiology and immunology [ 0385-5600 ] ; 2008.
Descripteurs français
- KwdFr :
- Humains, Logiciel, Mutagenèse dirigée, Mutation, Relation structure-activité, Sialidase (), Sialidase (génétique), Sialidase (métabolisme), Sous-type H3N2 du virus de la grippe A (), Sous-type H3N2 du virus de la grippe A (génétique), Sous-type H3N2 du virus de la grippe A (métabolisme), Substitution d'acide aminé, Séquence d'acides aminés.
- MESH :
- génétique : Sialidase, Sous-type H3N2 du virus de la grippe A.
- métabolisme : Sialidase, Sous-type H3N2 du virus de la grippe A.
- Humains, Logiciel, Mutagenèse dirigée, Mutation, Relation structure-activité, Sialidase, Sous-type H3N2 du virus de la grippe A, Substitution d'acide aminé, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Humans, Influenza A Virus, H3N2 Subtype (chemistry), Influenza A Virus, H3N2 Subtype (genetics), Influenza A Virus, H3N2 Subtype (metabolism), Mutagenesis, Site-Directed, Mutation, Neuraminidase (chemistry), Neuraminidase (genetics), Neuraminidase (metabolism), Software, Structure-Activity Relationship.
- MESH :
- chemical , chemistry : Neuraminidase.
- chemistry : Influenza A Virus, H3N2 Subtype.
- genetics : Influenza A Virus, H3N2 Subtype, Neuraminidase.
- metabolism : Influenza A Virus, H3N2 Subtype, Neuraminidase.
- Amino Acid Sequence, Amino Acid Substitution, Humans, Mutagenesis, Site-Directed, Mutation, Software, Structure-Activity Relationship.
Abstract
In order to clarify the effect of amino acid substitutions on the structure and function of the neuraminidase (NA) protein of influenza A virus, we introduced single-point amino acid substitutions into the NA protein of the A/Tokyo/3/67 (H2N2) strain using PCR-based random mutation. The rate of tolerant random one amino acid substitutions in the NA protein was 47%. Rates of tolerant substitutions for the stalk and for the surface and inner portion of the head region of the NA protein were 79, 54, and 19%, respectively. Deleterious changes, such as those causing the NA protein to stop at the Golgi/endoplasmic reticulum, were scattered throughout the protein. On the other hand, the ratio of mutations with which the NA protein lost neuraminidase activity, but was transported to the cell surface, decreased in proportion to the distance from the structural center of enzyme active site. In order to investigate the effect of accumulated amino acid substitutions on the structural character of the N2NA protein during evolution, the same amino acid substitutions were introduced by site-directed mutagenesis at 23 homologous positions on N2 proteins of A/Tokyo/3/67, A/Bangkok/15/85 (H3N2), and A/Mie/1/2004 (H3N2). The results showed a shift, or discordance, in tolerance at some of the positions. An increase in discordance was correlated with the interval in years between virus strains, and the discordance rate was estimated to be 0.6-0.7% per year.
DOI: 10.1111/j.1348-0421.2008.00034.x
PubMed: 18426396
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first="Setsuko" last="Nakajima">Setsuko Nakajima</name></author><author><name sortKey="Nakajima, Katsuhisa" sort="Nakajima, Katsuhisa" uniqKey="Nakajima K" first="Katsuhisa" last="Nakajima">Katsuhisa Nakajima</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18426396</idno><idno type="pmid">18426396</idno><idno type="doi">10.1111/j.1348-0421.2008.00034.x</idno><idno type="wicri:Area/PubMed/Corpus">000261</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000261</idno><idno type="wicri:Area/PubMed/Curation">000261</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000261</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Effects of single-point amino acid substitutions on the structure and function neuraminidase proteins in influenza A virus.</title><author><name sortKey="Yano, Takuya" sort="Yano, 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(génétique)</term><term>Sialidase (métabolisme)</term><term>Sous-type H3N2 du virus de la grippe A ()</term><term>Sous-type H3N2 du virus de la grippe A (génétique)</term><term>Sous-type H3N2 du virus de la grippe A (métabolisme)</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Influenza A Virus, H3N2 Subtype</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Influenza A Virus, H3N2 Subtype</term><term>Neuraminidase</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Sialidase</term><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><term>Neuraminidase</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" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Humans</term><term>Mutagenesis, Site-Directed</term><term>Mutation</term><term>Software</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Logiciel</term><term>Mutagenèse dirigée</term><term>Mutation</term><term>Relation structure-activité</term><term>Sialidase</term><term>Sous-type H3N2 du virus de la grippe A</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In order to clarify the effect of amino acid substitutions on the structure and function of the neuraminidase (NA) protein of influenza A virus, we introduced single-point amino acid substitutions into the NA protein of the A/Tokyo/3/67 (H2N2) strain using PCR-based random mutation. The rate of tolerant random one amino acid substitutions in the NA protein was 47%. Rates of tolerant substitutions for the stalk and for the surface and inner portion of the head region of the NA protein were 79, 54, and 19%, respectively. Deleterious changes, such as those causing the NA protein to stop at the Golgi/endoplasmic reticulum, were scattered throughout the protein. On the other hand, the ratio of mutations with which the NA protein lost neuraminidase activity, but was transported to the cell surface, decreased in proportion to the distance from the structural center of enzyme active site. In order to investigate the effect of accumulated amino acid substitutions on the structural character of the N2NA protein during evolution, the same amino acid substitutions were introduced by site-directed mutagenesis at 23 homologous positions on N2 proteins of A/Tokyo/3/67, A/Bangkok/15/85 (H3N2), and A/Mie/1/2004 (H3N2). The results showed a shift, or discordance, in tolerance at some of the positions. An increase in discordance was correlated with the interval in years between virus strains, and the discordance rate was estimated to be 0.6-0.7% per year.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18426396</PMID><DateCompleted><Year>2008</Year><Month>11</Month><Day>05</Day></DateCompleted><DateRevised><Year>2008</Year><Month>04</Month><Day>22</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0385-5600</ISSN><JournalIssue CitedMedium="Print"><Volume>52</Volume><Issue>4</Issue><PubDate><Year>2008</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Microbiology and immunology</Title><ISOAbbreviation>Microbiol. Immunol.</ISOAbbreviation></Journal><ArticleTitle>Effects of single-point amino acid substitutions on the structure and function neuraminidase proteins in influenza A virus.</ArticleTitle><Pagination><MedlinePgn>216-23</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1348-0421.2008.00034.x</ELocationID><Abstract><AbstractText>In order to clarify the effect of amino acid substitutions on the structure and function of the neuraminidase (NA) protein of influenza A virus, we introduced single-point amino acid substitutions into the NA protein of the A/Tokyo/3/67 (H2N2) strain using PCR-based random mutation. The rate of tolerant random one amino acid substitutions in the NA protein was 47%. Rates of tolerant substitutions for the stalk and for the surface and inner portion of the head region of the NA protein were 79, 54, and 19%, respectively. Deleterious changes, such as those causing the NA protein to stop at the Golgi/endoplasmic reticulum, were scattered throughout the protein. On the other hand, the ratio of mutations with which the NA protein lost neuraminidase activity, but was transported to the cell surface, decreased in proportion to the distance from the structural center of enzyme active site. In order to investigate the effect of accumulated amino acid substitutions on the structural character of the N2NA protein during evolution, the same amino acid substitutions were introduced by site-directed mutagenesis at 23 homologous positions on N2 proteins of A/Tokyo/3/67, A/Bangkok/15/85 (H3N2), and A/Mie/1/2004 (H3N2). The results showed a shift, or discordance, in tolerance at some of the positions. An increase in discordance was correlated with the interval in years between virus strains, and the discordance rate was estimated to be 0.6-0.7% per year.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yano</LastName><ForeName>Takuya</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Virology, Medical School, Nagoya City University, Nagoya, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nobusawa</LastName><ForeName>Eri</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Nagy</LastName><ForeName>Alexander</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Nakajima</LastName><ForeName>Setsuko</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Nakajima</LastName><ForeName>Katsuhisa</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Australia</Country><MedlineTA>Microbiol Immunol</MedlineTA><NlmUniqueID>7703966</NlmUniqueID><ISSNLinking>0385-5600</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 3.2.1.18</RegistryNumber><NameOfSubstance UI="D009439">Neuraminidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="Y">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053122" MajorTopicYN="N">Influenza A Virus, H3N2 Subtype</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="Y">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009439" MajorTopicYN="N">Neuraminidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012984" MajorTopicYN="N">Software</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>4</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>11</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>4</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18426396</ArticleId><ArticleId IdType="pii">MIM034</ArticleId><ArticleId IdType="doi">10.1111/j.1348-0421.2008.00034.x</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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