title: Host sialoglycans and bacterial sialidases: a mucosal perspective.
abstract: Sialic acids are nine-carbon-backbone sugars that occupy outermost positions on vertebrate cells and secreted sialoglycoproteins. These negatively charged hydrophilic carbohydrates have a variety of biological, biophysical and immunological functions. Mucosal surfaces and secretions of the mouth, airway, gut and vagina are especially sialoglycan-rich. Given their prominent positions and important functions, a variety of microbial strategies have targeted host sialic acids for adherence, mimicry and/or degradation. Here we review the roles of bacterial sialidases (neuraminidases) during colonization and pathogenesis of mammalian mucosal surfaces. Evidence is presented to support the myriad roles of mucosal sialoglycans in protecting the host from bacterial infection. In opposition, many bacteria hydrolyse sialic acids during associations with the gastrointestinal, oral, respiratory and reproductive tracts. Sialidases promote bacterial survival in mucosal niche environments in several ways, including: (i) nutritional benefits of sialic acid catabolism, (ii) unmasking of cryptic host ligands used for adherence, (iii) participation in biofilm formation and (iv) modulation of immune function. Bacterial sialidases are among the best-studied enzymes involved in pathogenesis and may also drive commensal and/or symbiotic host associations. Future studies should continue to define host substrates of bacterial sialidases and the mechanisms of their pathologic, commensal and symbiotic interactions with the mammalian host.
authors.affiliation: Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO, USA. allewis@wustl.edu
authors.forename: Amanda L
authors.initials: AL
authors.lastname: Lewis
authors.forename: Warren G
authors.initials: WG
authors.lastname: Lewis
mesh_terms: D000818:Animals; D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins; D002240:Carbohydrate Sequence; D054884:Host-Pathogen Interactions; D006801:Humans; D008969:Molecular Sequence Data; D009088:Mucoproteins; D009092:Mucous Membrane / Q000378:metabolism / Q000382:microbiology*; D009439:Neuraminidase; D009844:Oligosaccharides / Q000378:metabolism / Q000502:physiology*; D012794:Sialic Acids / Q000378:metabolism / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; D009088:Mucoproteins; D009844:Oligosaccharides; D012794:Sialic Acids; D009439:Neuraminidase