Isolation and characterization of gluten degrading enzymes derived from Rothia species

PLEASE NOTE: This work is protected by copyright. Downloading is restricted to the BU community: please click Download and log in with a valid BU account to access. If you are the author of this work and would like to make it publicly available, please contact open-help@bu.edu.Thesis (MSD) --Boston University, Henry M. Goldman School of Dental Medicine, 2012 (Department of Periodontology and Oral Biology).Includes bibliography: leaves 58-65.Celiac disease (CD) is an inflammatory enteropathy of the small intestine, which affects certain genetically predisposed individuals. The disease is triggered upon ingestion of wheat gluten and similar proteins found in other cereals such as barley and rye. Once diagnosed, celiac patients must adhere strictly to a gluten free diet, since no true therapy is currently available. The gliadin fractions of gluten proteins contain multiple T-cell epitopes within their primary structure. These domains are responsible for the high immunogenicity presented by the gliadin fractions upon ingestion. The human-encoded enzymatic arsenal lacks cleavage capacities towards these peptides. For this reason, the use of external gliadin-degrading proteases has been proposed as a therapeutic alternative for the treatment of CD. [TRUNCATED