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

FEBS Lett. 2003 May 22;543(1-3):71-5. doi: 10.1016/s0014-5793(03)00403-4.

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.

MeSH terms

  • 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

Substances

  • Amino Acids
  • Recombinant Fusion Proteins
  • Neuraminidase

Associated data

  • GENBANK/AB101671
  • GENBANK/AB101672
  • GENBANK/AB101673
  • GENBANK/AB101674
  • GENBANK/AB101675