The sialidase superfamily and its spread by horizontal gene transfer

Mol Microbiol. 1993 Sep;9(5):915-21. doi: 10.1111/j.1365-2958.1993.tb01221.x.

Abstract

Sialidases (neuraminidases, EC 3.2.1.18) belong to a class of glycosyl hydrolases that release terminal N-acylneuraminate (sialic acid) residues from glycoproteins, glycolipids, and polysaccharides. These enzymes are common in animals of the deuterostomate lineage (Echinodermata through Mammalia) and also in diverse microorganisms that mostly exist as animal commensals or pathogens. Sialidases, and their sialyl substrates, appear to be absent from plants and most other metazoans. Even among bacteria, sialidase is found irregularly so that related species or even strains of one species differ in this property. This unusual phylogenetic distribution makes sialidases interesting for evolutionary studies. The biochemical diversity among bacterial sialidases does not indicate close relationships. However, at the molecular level, homologies are detectable, supporting the hypothesis of a common sialidase origin and thus of a sialidase superfamily. Some findings indicate that sialidase genes were recently transferred via phages among bacteria. The proposal of a sialidase origin in higher animals is suggested by the presence of apparently homologous enzymes in this kingdom, supporting the idea that some microbes may have acquired the genetic information during association with their animal hosts.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacteria / enzymology*
  • Bacteria / genetics
  • Gene Transfer, Horizontal*
  • Genes, Bacterial*
  • Isoenzymes / chemistry
  • Isoenzymes / genetics
  • Molecular Sequence Data
  • Multigene Family*
  • Neuraminidase / chemistry
  • Neuraminidase / genetics*
  • Sequence Homology, Amino Acid

Substances

  • Isoenzymes
  • Neuraminidase