A molecular mechanism for the low-pH stability of sialidase activity of influenza A virus N2 neuraminidases.
Identifieur interne : 000339 ( PubMed/Corpus ); précédent : 000338; suivant : 000340A molecular mechanism for the low-pH stability of sialidase activity of influenza A virus N2 neuraminidases.
Auteurs : Tadanobu Takahashi ; Takashi Suzuki ; Kazuya I-P Jwa Hidari ; Daisei Miyamoto ; Yasuo SuzukiSource :
- FEBS letters [ 0014-5793 ] ; 2003.
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
Links to Exploration step
pubmed:12753908Le document en format XML
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<author><name sortKey="Suzuki, Takashi" sort="Suzuki, Takashi" uniqKey="Suzuki T" first="Takashi" last="Suzuki">Takashi Suzuki</name>
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<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>
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<author><name sortKey="Miyamoto, Daisei" sort="Miyamoto, Daisei" uniqKey="Miyamoto D" first="Daisei" last="Miyamoto">Daisei Miyamoto</name>
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<author><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name>
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
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