All major cholesterol-dependent cytolysins use glycans as cellular receptors
Lucy K. Shewell, Christopher J. Day, Freda E.‐C. Jen, Thomas Haselhorst, John M. Atack, Josephine F. Reijneveld, Arun Everest‐Dass, David B. A. James, Kristina M. Boguslawski, Stephan Brouwer, Christine M. Gillen, Zhenyao Luo, Boštjan Kobe, Victor Nizet, Mark von Itzstein, Mark J. Walker, Adrienne W. Paton, James C. Paton, Victor J. Torres, Michael P. Jennings
Abstract
-glycan on its erythrocyte receptor, CD59. Removing sialyl-TF from CD59 reduces intermedilysin binding. Glycan-lectin interactions underpin the cellular tropism of CDCs and provide molecular targets to block their cytotoxic activity.
Topics & Concepts
GlycanReceptorCytotoxicityCholesterolCell biologyChemistryBiologyBiochemistryGlycoproteinIn vitroGlycosylation and Glycoproteins ResearchPancreatic function and diabetesMonoclonal and Polyclonal Antibodies Research