Recent development in mammalian sialidase molecular biology

Neurochem Res. 2002 Aug;27(7-8):649-63. doi: 10.1023/a:1020276000901.


This review summarizes the recent research development on mammalian sialidase molecular cloning. Sialic acid-containing compounds are involved in several physiological processes, and sialidases, as glycohydrolytic enzymes that remove sialic acid residues, play a pivotal role as well. Sialidases hydrolyze the nonreducing, terminal sialic acid linkage in various natural substrates, such as glycoproteins, glycolipids, gangliosides, and polysaccharides. Mammalian sialidases are present in several tissues/organs and cells with a typical subcellular distribution: they are the lysosomal, the cytosolic, and the plasma membrane-associated sialidases. Starting in 1993, 12 different mammalian sialidases have been cloned and sequenced. A comparison of their amino acid sequences revealed the presence of highly conserved regions. These conserved regions are shared with viral and microbial sialidases that have been characterized at three-dimensional structural level, allowing us to perform the molecular modeling of the mammalian proteins and suggesting a monophyletic origin of the sialidase enzymes. Overall, the availability of the cDNA species encoding mammalian sialidases is an important step leading toward a comprehensive picture of the relationships between the structure and biological function of these enzymes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Differentiation / physiology
  • Cell Membrane / enzymology
  • Cloning, Molecular
  • Humans
  • Mammals
  • Molecular Sequence Data
  • Mucolipidoses / enzymology
  • Mutagenesis, Site-Directed
  • Neoplasms / enzymology
  • Neuraminidase / chemistry
  • Neuraminidase / genetics*
  • Neuraminidase / physiology
  • Sequence Homology, Amino Acid
  • Transfection


  • Neuraminidase

Associated data

  • OMIM/256540
  • OMIM/256550