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Toll-Like Receptor 11 (TLR11) Interacts with Flagellin and Profilin through Disparate Mechanisms
Authors:Hirotsugu Hatai  Alice Lepelley  Wangyong Zeng  Matthew S. Hayden  Sankar Ghosh
Affiliation:1. Department of Microbiology & Immunology, College of Physicians & Surgeons, Columbia University, New York, New York, United States of America;2. Department of Pathology, Immunology and Microbiology, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo, Japan;3. Department of Dermatology, College of Physicians & Surgeons, Columbia University, New York, New York, United States of America;University at Buffalo, UNITED STATES
Abstract:Toll-like receptors (TLRs) are innate immune receptors that sense a variety of pathogen-associated molecular patterns (PAMPs) by interacting with them and subsequently initiating signal transduction cascades that elicit immune responses. TLR11 has been shown to interact with two known protein PAMPs: Salmonella and E. coli flagellin FliC and Toxoplasma gondii profilin-like protein. Given the highly divergent biology of these pathogens recognized by TLR11, it is unclear whether common mechanisms are used to recognize these distinct protein PAMPs. Here we show that TLR11 interacts with these two PAMPs using different receptor domains. Furthermore, TLR11 binding to flagellin and profilin exhibits differential dependency on pH and receptor ectodomain cleavage.
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