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A molecular mechanism for the low‐pH stability of sialidase activity of influenza A virus N2 neuraminidases 1
Author(s) -
Takahashi Tadanobu,
Suzuki Takashi,
Hidari Kazuya I.-P.Jwa,
Miyamoto Daisei,
Suzuki Yasuo
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00403-4
Subject(s) - sialidase , neuraminidase , virus , chemistry , amino acid , influenza a virus , pandemic , biochemistry , virology , covid-19 , biology , medicine , disease , pathology , infectious disease (medical specialty)
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.