A molecular mechanism for the low-pH stability of sialidase activity of influenza A virus N2 neuraminidases.
Identifieur interne : 000125 ( 1968/Analysis ); précédent : 000124; suivant : 000126A molecular mechanism for the low-pH stability of sialidase activity of influenza A virus N2 neuraminidases.
Auteurs : Tadanobu Takahashi [Japon] ; Takashi Suzuki ; Kazuya I-P Jwa Hidari ; Daisei Miyamoto ; Yasuo SuzukiSource :
- FEBS letters [ 0014-5793 ] ; 2003.
Descripteurs français
- KwdFr :
- Acides aminés (analyse), Concentration en ions d'hydrogène, Données de séquences moléculaires, Humains, Lignée cellulaire, Modèles moléculaires, Protéines de fusion recombinantes (métabolisme), Sialidase (), Sialidase (génétique), Sialidase (métabolisme), Stabilité enzymatique, Substitution d'acide aminé, Séquence nucléotidique, Virus de la grippe A (enzymologie).
- MESH :
- analyse : Acides aminés.
- enzymologie : Virus de la grippe A.
- génétique : Sialidase.
- métabolisme : Protéines de fusion recombinantes, Sialidase.
- Concentration en ions d'hydrogène, Données de séquences moléculaires, Humains, Lignée cellulaire, Modèles moléculaires, Sialidase, Stabilité enzymatique, Substitution d'acide aminé, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Substitution, Amino Acids (analysis), Base Sequence, Cell Line, Enzyme Stability, Humans, Hydrogen-Ion Concentration, Influenza A virus (enzymology), Models, Molecular, Molecular Sequence Data, Neuraminidase (chemistry), Neuraminidase (genetics), Neuraminidase (metabolism), Recombinant Fusion Proteins (metabolism).
- MESH :
- chemical , analysis : Amino Acids.
- chemical , chemistry : Neuraminidase.
- enzymology : Influenza A virus.
- chemical , genetics : Neuraminidase.
- chemical , metabolism : Neuraminidase, Recombinant Fusion Proteins.
- Amino Acid Substitution, Base Sequence, Cell Line, Enzyme Stability, Humans, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data.
Abstract
Four human pandemic influenza A virus strains isolated in 1957 and 1968, but not most of the epidemic strains isolated after 1968, possess sialidase activity under low-pH conditions. Here, we used cell-expressed neuraminidases (NAs) to determine the region of the N2 NA that is associated with low-pH stability of sialidase activity. We found that consensus amino acid regions responsible for low-pH stability did not exist in pandemic NAs but that two amino acid substitutions in the low-pH-stable A/Hong Kong/1/68 (H3N2) NA and a single substitution in the low-pH-unstable A/Texas/68 (H2N2) NA resulted in significant change in low-pH stability.
DOI: 10.1016/s0014-5793(03)00403-4
PubMed: 12753908
Affiliations:
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pubmed:12753908Le document en format XML
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University of Shizuoka, School of Pharmaceutical Sciences, CREST, JST, and COE Program in the 21st Century, 422-8526, Shizuoka, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Sciences, CREST, JST, and COE Program in the 21st Century, 422-8526, Shizuoka</wicri:regionArea><wicri:noRegion>Shizuoka</wicri:noRegion></affiliation></author><author><name sortKey="Suzuki, Takashi" sort="Suzuki, Takashi" uniqKey="Suzuki T" first="Takashi" last="Suzuki">Takashi Suzuki</name></author><author><name sortKey="Hidari, Kazuya I P Jwa" sort="Hidari, Kazuya I P Jwa" uniqKey="Hidari K" first="Kazuya I-P Jwa" last="Hidari">Kazuya I-P Jwa Hidari</name></author><author><name sortKey="Miyamoto, Daisei" sort="Miyamoto, Daisei" uniqKey="Miyamoto D" first="Daisei" last="Miyamoto">Daisei Miyamoto</name></author><author><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>Amino Acids (analysis)</term><term>Base Sequence</term><term>Cell Line</term><term>Enzyme Stability</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Influenza A virus (enzymology)</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Neuraminidase (chemistry)</term><term>Neuraminidase (genetics)</term><term>Neuraminidase (metabolism)</term><term>Recombinant Fusion Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (analyse)</term><term>Concentration en ions d'hydrogène</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Lignée 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Here, we used cell-expressed neuraminidases (NAs) to determine the region of the N2 NA that is associated with low-pH stability of sialidase activity. We found that consensus amino acid regions responsible for low-pH stability did not exist in pandemic NAs but that two amino acid substitutions in the low-pH-stable A/Hong Kong/1/68 (H3N2) NA and a single substitution in the low-pH-unstable A/Texas/68 (H2N2) NA resulted in significant change in low-pH stability.</div></front></TEI><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Hidari, Kazuya I P Jwa" sort="Hidari, Kazuya I P Jwa" uniqKey="Hidari K" first="Kazuya I-P Jwa" last="Hidari">Kazuya I-P Jwa Hidari</name><name sortKey="Miyamoto, Daisei" sort="Miyamoto, Daisei" uniqKey="Miyamoto D" first="Daisei" last="Miyamoto">Daisei Miyamoto</name><name sortKey="Suzuki, Takashi" sort="Suzuki, Takashi" uniqKey="Suzuki T" first="Takashi" last="Suzuki">Takashi Suzuki</name><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name></noCountry><country name="Japon"><noRegion><name sortKey="Takahashi, Tadanobu" sort="Takahashi, Tadanobu" uniqKey="Takahashi T" first="Tadanobu" last="Takahashi">Tadanobu Takahashi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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