|
Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Dental Medicine / Faculty of Dental Medicine >
Peer-reviewed Journal Articles, etc >
CD14 directly binds to triacylated lipopeptides and facilitates recognition of the lipopeptides by the receptor complex of Toll-like receptors 2 and 1 without binding to the complex
| Title: | CD14 directly binds to triacylated lipopeptides and facilitates recognition of the lipopeptides by the receptor complex of Toll-like receptors 2 and 1 without binding to the complex |
| Authors: | Nakata, Takashi Browse this author | | Yasuda, Motoaki Browse this author | | Fujita, Mari Browse this author | | Kataoka, Hideo Browse this author | | Kiura, Kazuto Browse this author | | Sano, Hidehiko Browse this author →KAKEN DB | | Shibata, Kenichiro Browse this author →KAKEN DB |
| Issue Date: | Dec-2006 |
| Publisher: | Blackwell Publishing |
| Journal Title: | Cellular Microbiology |
| Volume: | 8 |
| Issue: | 12 |
| Start Page: | 1899 |
| End Page: | 1909 |
| Publisher DOI: | 10.1111/j.1462-5822.2006.00756.x |
| PMID: | 16848791 |
| Abstract: | It has demonstrated that the recognition of triacylated lipopeptides by Toll-like receptor (TLR) 2 requires TLR1 as a coreceptor. In the NF-κB reporter assay system in which human embryonic kidney 293 cells were transfected with TLR2 and TLR1 together with an NF-κB luciferase reporter gene, S-(2,3-bispalmitoyloxypropyl)-N-palmitoyl-Cys-Lys-Lys-Lys-Lys (Pam3CSK4) and Pam3CSSNA were recognized by TLR2/TLR1, but the recognition level was unexpectedly very low. However, cotransfection of CD14 drastically enhanced the recognition of triacylated lipopeptides by TLR2/TLR1. The CD14-induced enhancement did not occur without cotransfection of TLR1. Both CD14dS39-A48, a mutant with deletion of the part of possible N-terminal ligand-binding pocket, and anti-CD14 monoclonal antibody reduced the CD14-induced enhancement. Transfection of a TIR domain-deficient mutant of TLR2 (TLR2dE772-S784) or TLR1 (TLR1dQ636-K779) completely abrogated the CD14-induced enhancement. Soluble recombinant CD14 added extracellularly enhanced the recognition of Pam3CSSNA by TLR2/TLR1. Immunoprecipitation analysis demonstrated that CD14 was not associated with TLR2 but that TLR1 was associated with TLR2. In addition, surface plasmon resonance-based assay demonstrated that CD14 binds to Pam3CSK4 at a dissociation constant of 5.7 µM. This study suggests that CD14 directly binds to triacylated lipopeptides and facilitates recognition of the lipopeptides by the TLR2/TLR1 complex without binding to the receptor complex. |
| Rights: | The definitive version is available at www.blackwell-synergy.com |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/30223 |
| Appears in Collections: | 歯学院・歯学研究院 (Graduate School of Dental Medicine / Faculty of Dental Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
Submitter: 柴田 健一郎
|
