Low-pH Stability of Influenza A Virus Sialidase Contributing to Virus Replication and Pandemic.
Identifieur interne : 000031 ( 1968/Analysis ); précédent : 000030; suivant : 000032Low-pH Stability of Influenza A Virus Sialidase Contributing to Virus Replication and Pandemic.
Auteurs : Tadanobu Takahashi ; Takashi SuzukiSource :
- Biological & pharmaceutical bulletin [ 1347-5215 ] ; 2015.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Virus de la grippe A.
- génétique : Protéines virales, Sialidase.
- pathogénicité : Virus de la grippe A.
- virologie : Grippe humaine.
- épidémiologie : Grippe humaine.
- Humains, Pandémies, Protéines virales, Réplication virale, Sialidase, Substitution d'acide aminé.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Neuraminidase, Viral Proteins.
- enzymology : Influenza A virus.
- epidemiology : Influenza, Human.
- chemical , genetics : Neuraminidase, Viral Proteins.
- pathogenicity : Influenza A virus.
- virology : Influenza, Human.
- Amino Acid Substitution, Humans, Pandemics, Virus Replication.
Abstract
The spike glycoprotein neuraminidase (NA) of influenza A virus (IAV) has sialidase activity that cleaves the terminal sialic acids (viral receptors) from oligosaccharide chains of glycoconjugates. A new antigenicity of viral surface glycoproteins for humans has pandemic potential. We found "low-pH stability of sialidase activity" in NA. The low-pH stability can maintain sialidase activity under acidic conditions of pH 4-5. For human IAVs, NAs of all pandemic viruses were low-pH-stable, whereas those of almost all human seasonal viruses were not. The low-pH stability was dependent on amino acid residues near the active site, the calcium ion-binding site, and the subunit interfaces of the NA homotetramer, suggesting effects of the active site and the homotetramer on structural stability. IAVs with the low-pH-stable NA showed much higher virus replication rates than those of IAVs with low-pH-unstable NA, which was correlated with maintenance of sialidase activity under an endocytic pathway of the viral cell entry mechanism, indicating contribution of low-pH stability to high replication rates of pandemic viruses. The low-pH-stable NA of the 1968 H3N2 pandemic virus was derived from the low-pH-stable NA of H2N2 human seasonal virus, one of two types classified by both low-pH stability in N2 NA and a phylogenetic tree of N2 NA genes. The 2009 H1N1 pandemic virus acquired low-pH-stable NA by two amino acid substitutions at the early stage of the 2009 pandemic. It is thought that low-pH stability contributes to infection spread in a pandemic through enhancement of virus replication.
DOI: 10.1248/bpb.b15-00120
PubMed: 26027822
Affiliations:
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pubmed:26027822Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Low-pH Stability of Influenza A Virus Sialidase Contributing to Virus Replication and Pandemic.</title><author><name sortKey="Takahashi, Tadanobu" sort="Takahashi, Tadanobu" uniqKey="Takahashi T" first="Tadanobu" last="Takahashi">Tadanobu Takahashi</name><affiliation><nlm:affiliation>Department of Biochemistry, School of Pharmaceutical Sciences,
University of Shizuoka.</nlm:affiliation><wicri:noCountry code="subField">
University of Shizuoka</wicri:noCountry></affiliation></author><author><name sortKey="Suzuki, Takashi" sort="Suzuki, Takashi" uniqKey="Suzuki T" first="Takashi" last="Suzuki">Takashi Suzuki</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26027822</idno><idno type="pmid">26027822</idno><idno type="doi">10.1248/bpb.b15-00120</idno><idno type="wicri:Area/PubMed/Corpus">000074</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000074</idno><idno type="wicri:Area/PubMed/Curation">000074</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000074</idno><idno type="wicri:Area/PubMed/Checkpoint">000066</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000066</idno><idno type="wicri:Area/Ncbi/Merge">000B68</idno><idno type="wicri:Area/Ncbi/Curation">000B68</idno><idno type="wicri:Area/Ncbi/Checkpoint">000B68</idno><idno type="wicri:Area/Main/Merge">000550</idno><idno type="wicri:Area/Main/Curation">000549</idno><idno type="wicri:Area/Main/Exploration">000549</idno><idno type="wicri:Area/1968/Extraction">000031</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Low-pH Stability of Influenza A Virus Sialidase Contributing to Virus Replication and Pandemic.</title><author><name sortKey="Takahashi, Tadanobu" sort="Takahashi, Tadanobu" uniqKey="Takahashi T" first="Tadanobu" last="Takahashi">Tadanobu Takahashi</name><affiliation><nlm:affiliation>Department of Biochemistry, School of Pharmaceutical Sciences,
University of Shizuoka.</nlm:affiliation><wicri:noCountry code="subField">
University of Shizuoka</wicri:noCountry></affiliation></author><author><name sortKey="Suzuki, Takashi" sort="Suzuki, Takashi" uniqKey="Suzuki T" first="Takashi" last="Suzuki">Takashi Suzuki</name></author></analytic><series><title level="j">Biological & pharmaceutical bulletin</title><idno type="eISSN">1347-5215</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>Humans</term><term>Influenza A virus (enzymology)</term><term>Influenza A virus (pathogenicity)</term><term>Influenza, Human (epidemiology)</term><term>Influenza, Human (virology)</term><term>Neuraminidase (chemistry)</term><term>Neuraminidase (genetics)</term><term>Pandemics</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (genetics)</term><term>Virus Replication</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Grippe humaine (virologie)</term><term>Grippe humaine (épidémiologie)</term><term>Humains</term><term>Pandémies</term><term>Protéines virales ()</term><term>Protéines virales (génétique)</term><term>Réplication virale</term><term>Sialidase ()</term><term>Sialidase (génétique)</term><term>Substitution d'acide aminé</term><term>Virus de la grippe A (enzymologie)</term><term>Virus de la grippe A (pathogénicité)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Neuraminidase</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="epidemiology" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Neuraminidase</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines virales</term><term>Sialidase</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Grippe humaine</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="épidémiologie" xml:lang="fr"><term>Grippe humaine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Humans</term><term>Pandemics</term><term>Virus Replication</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Pandémies</term><term>Protéines virales</term><term>Réplication virale</term><term>Sialidase</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The spike glycoprotein neuraminidase (NA) of influenza A virus (IAV) has sialidase activity that cleaves the terminal sialic acids (viral receptors) from oligosaccharide chains of glycoconjugates. A new antigenicity of viral surface glycoproteins for humans has pandemic potential. We found "low-pH stability of sialidase activity" in NA. The low-pH stability can maintain sialidase activity under acidic conditions of pH 4-5. For human IAVs, NAs of all pandemic viruses were low-pH-stable, whereas those of almost all human seasonal viruses were not. The low-pH stability was dependent on amino acid residues near the active site, the calcium ion-binding site, and the subunit interfaces of the NA homotetramer, suggesting effects of the active site and the homotetramer on structural stability. IAVs with the low-pH-stable NA showed much higher virus replication rates than those of IAVs with low-pH-unstable NA, which was correlated with maintenance of sialidase activity under an endocytic pathway of the viral cell entry mechanism, indicating contribution of low-pH stability to high replication rates of pandemic viruses. The low-pH-stable NA of the 1968 H3N2 pandemic virus was derived from the low-pH-stable NA of H2N2 human seasonal virus, one of two types classified by both low-pH stability in N2 NA and a phylogenetic tree of N2 NA genes. The 2009 H1N1 pandemic virus acquired low-pH-stable NA by two amino acid substitutions at the early stage of the 2009 pandemic. It is thought that low-pH stability contributes to infection spread in a pandemic through enhancement of virus replication. </div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Suzuki, Takashi" sort="Suzuki, Takashi" uniqKey="Suzuki T" first="Takashi" last="Suzuki">Takashi Suzuki</name><name sortKey="Takahashi, Tadanobu" sort="Takahashi, Tadanobu" uniqKey="Takahashi T" first="Tadanobu" last="Takahashi">Tadanobu Takahashi</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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