A molecular mechanism for the low‐pH stability of sialidase activity of influenza A virus N2 neuraminidases

FEBS Letters

Miyamoto, Daisei¹  Suzuki, Takashi¹  Suzuki, Yasuo¹  Hidari, Kazuya I.-P.Jwa¹  Takahashi, Tadanobu¹ 

[1] Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Sciences, CREST, JST, and COE Program in the 21 Century, Shizuoka 422-8526, Japan

关键词: Chimera;    Influenza virus;    Low-pH stability;    Molecular mechanism;    Neuraminidase;    Sialidase;    FBS;    fetal bovine serum;    MEM;    minimum essential medium;    4-MUα-Neu5Ac;    2′-(4-methylumbelliferyl)-α-D-N-acetylneuraminic acid;    NA;    neuraminidase;    PBS;    phosphate-buffered saline;   

DOI  :  10.1016/S0014-5793(03)00403-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown