The sialidase superfamily and its spread by horizontal gene transfer

Peter Roggentin, Roland Schauer, Lois L. Hoyer, Eric R. Vimr

Research output: Contribution to journalArticlepeer-review

Abstract

Sialidases (neuraminidases, EC 3.2.1.18) belong to a class of glycosyl hydrolases that release terminal N‐acylneuraminate (slalic 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 super family. 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.

Original languageEnglish (US)
Pages (from-to)915-921
Number of pages7
JournalMolecular Microbiology
Volume9
Issue number5
DOIs
StatePublished - Sep 1993

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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