Epithelial surfaces throughout the body are coated by mucins, a class of proteins carrying domains characterized by a high density of O-glycosylated serine and threonine residues. The resulting mucosal layers form crucial host-microbe interfaces that prevent the translocation of microbes while also selecting for distinct bacteria via the presented glycan repertoire. The intricate interplay between mucus production and breakdown thus determines the composition of the microbiota maintained within these mucosal environments, which can have a large influence on the host during both homeostasis and disease. Most research to date on mucus breakdown has focused on glycosidases that trim glycan structures to release monosaccharides as a source of nutrients. More recent work has uncovered the existence of mucin-type O-glycosylation-dependent proteases that are secreted by pathogens, commensals, and mutualists to facilitate mucosal colonization and penetration. Additionally, immunoglobulin A (IgA) proteases promote bacterial colonization in the presence of neutralizing secretory IgA through selective cleavage of the heavily O-glycosylated hinge region. In this review, we summarize families of O-glycoproteases and IgA proteases, discuss known structural features, and review applications of these enzymes to glycobiology.
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Cover Image
Cover Image
Serine pyrophosphorylation by the inositol pyrophosphate 5-IP7 keeps cellular MYC levels in check. Elevation in MYC downstream to 5-IP7 depletion influences cell fate in response to environmental cues. For further information see the article in this issue by Lolla and colleagues (pp. 1647–1661). Image was created by Akruti Shah using BioRender.
Classification, structural biology, and applications of mucin domain-targeting proteases
D. Judy Shon, Angel Kuo, Michael J. Ferracane, Stacy A. Malaker; Classification, structural biology, and applications of mucin domain-targeting proteases. Biochem J 30 April 2021; 478 (8): 1585–1603. doi: https://doi.org/10.1042/BCJ20200607
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