Toll-Like Receptor 11 (TLR11) Interacts with Flagellin and Profilin through Disparate Mechanisms

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:...

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Bibliographic Details
Published in:PloS one 2016-02, Vol.11 (2), p.e0148987-e0148987
Main Authors: Hatai, Hirotsugu, Lepelley, Alice, Zeng, Wangyong, Hayden, Matthew S, Ghosh, Sankar
Format: Article
Language:English
Subjects:
Analysis
Animals
Biology and Life Sciences
Blotting, Western
Cascades
Cathepsins - metabolism
Cellular signal transduction
Cloning
Cloning, Molecular
Deoxyribonucleic acid
Dermatology
DNA
E coli
Flagellin
Flagellin - metabolism
Gene expression
HEK293 Cells
Humans
Immune response
Immune system
Immunology
Infections
Infectious diseases
Ligands
Mammals
Medicine and Health Sciences
Mice
Mutagenesis
Parasites
Pathogens
pH effects
Profilin
Profilins - metabolism
Protein Interaction Domains and Motifs
Proteins
Receptors
Recombinant Proteins
Research and Analysis Methods
Salmonella
Signal transduction
Surgeons
Toll-like receptors
Toll-Like Receptors - immunology
Toxoplasma
Toxoplasma gondii
Western blotting
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0148987