Year: 2018
Type: review
Abstract: The incidence of Clostridium difficile infection (CDI) has increased significantly worldwide, causing substantial morbidity and mortality. One of the major virulence factor, TcdB, manages to enter the colonic epithelia via the human frizzled proteins (FZDs), which are physiological receptors for Wnt morphogens. Binding of TcdB to FZDs inhibits Wnt signaling, which may contribute to pathogenesis of CDI. Here, we review the structural mechanism by which TcdB exploits to recognize FZDs for cell entry and inhibiting Wnt signaling, which reveals new strategies to modulate Wnt signaling for therapeutic interventions.
Source: FEBS Journal
DOI: 10.1111/febs.14681
Authors: Peng Chen, Liang Tao, Zheng Liu, Min Dong, Rongsheng Jin
Language: English
Subfield: Infectious Diseases
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
Funders: Boston Children's Hospital, National Institutes of Health, Intellectual and Developmental Disabilities Research Center, Harvard Digestive Diseases Center, Harvard University, National Cancer Institute, National Institute of Allergy and Infectious Diseases, National Institute of Diabetes and Digestive and Kidney Diseases, National Institute of Neurological Disorders and Stroke, Eunice Kennedy Shriver National Institute of Child Health and Human Development
Awards: G1721990140, G332990701, G4209746191, Novel anti-cancer biologics targeting Wnt signaling pathway, Structural mechanism for recognition of host receptor by botulinum neurotoxin A, G5857948765, Molecular mechanisms of botulinum neurotoxin neutralization, Structure and Function of C. Difficile Toxins, Molecular basis of action and pathogenesis of Clostridium difficile toxin B, Intellectual and Developmental Disablities Research Center, Integrated Epithelial and Muscosal Biology, Biology and Engineering of Botulinum Neurotoxins.
OpenAlex ID: W2897952042