The mucin-selective protease StcE enables molecular and functional analysis of human cancer-associated mucins

• DOI: 10.1073/pnas.1813020116
• Publication Date: 2019-03-26T00:28:46Z
• Authors: Stacy A. Malaker; Kayvon Pedram; Michael J. Ferracane; Barbara A. Bensing; Venkatesh Krishnan; Christian Pett; Jin Yu; Elliot C. Woods; Jessica R. Kramer; Ulrika Westerlind; Oliver Dorigo; Carolyn R. Bertozzi
• Keywords: 0301 basic medicine; Amino Acid Motifs; Antigens, Differentiation, Myelomonocytic; Mass Spectrometry; Substrate Specificity; 03 medical and health sciences; mucin; Antigens, CD; Lectins; Escherichia coli; glycoproteomics; Humans; Antigens; O-glycosylation; Sialic Acid Binding Immunoglobulin-like Lectins; Escherichia coli Proteins; Mucins; Metalloendopeptidases; protease; Myelomonocytic; CD; Neoplasm Proteins; 3. Good health; Siglec; Differentiation

Significance Mucin-domain glycoproteins are found in nearly every tissue of the human body, and are important in biological processes ranging from embryogenesis to cancer. Because there are few tools to study mucin domains, their biological functions at the molecular scale remain unclear. Here, we help address a hurdle to the study of mucin-domain glycoproteins by characterizing a bacterial protease with selectivity for mucins. This mucinase selectively removes native mucins from cell surfaces and cuts them into fragments amenable to analysis.