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Roles of N-linked glycans in the recognition of microbial lipopeptides and lipoproteins by TLR2
Title: | Roles of N-linked glycans in the recognition of microbial lipopeptides and lipoproteins by TLR2 |
Authors: | Kataoka, Hideo Browse this author | Yasuda, Motoaki Browse this author | Iyori, Mitsuhiro Browse this author | Kiura, Kazuto Browse this author | Narita, Mitsuo Browse this author | Nakata, Takashi Browse this author | Shibata, Ken-ichiro Browse this author →KAKEN DB |
Keywords: | Toll-like receptor 2 | N-linked glycans | FSL-1 | mycoplasmal lipoproteins |
Issue Date: | Jul-2006 |
Publisher: | Blackwell Publishing |
Journal Title: | Cellular Microbiology |
Volume: | 8 |
Issue: | 7 |
Start Page: | 1199 |
End Page: | 1209 |
Publisher DOI: | 10.1111/j.1462-5822.2006.00702.x |
PMID: | 16819971 |
Abstract: | Details of roles of carbohydrates attached to Toll-like receptors (TLRs) in the recognition of pathogen-associated molecular patterns and in the formation of the functional receptor complex still remain unknown. This study was designed to determine whether the glycans linked at Asn114, Asn199, Asn414 and Asn442 residues of TLR2 ectodomain were involved in the recognition of diacylated lipopeptide and lipoprotein. Single and multiple mutants were transfected into human embryonic kidney (HEK) 293 cells together with a NF-κB luciferase reporter plasmid. All of these mutants were expressed on the surface. SDS-PAGE of the transfectants demonstrated that these mutants migrated lower than wild-type TLR2 and their molecular masses decreased as the number of mutated Asn residues increased. TLR2N114A, TLR2N199A and TLR2N414A as well as wild-type TLR2 induced NF-κB activation when stimulated with these ligands, whereas TLR2N442A failed to induce NF-κB activation. All of triple and quadruple mutants failed to induce NF-κB activation, but were associated with both wild-type TLR2 and TLR6 in the transfectants. TLR2N114A,N199A, TLR2N114A,N414A and, to a lesser extent, TLR2N114A,N442A, in which two N-linked glycans are speculated to be exposed to the concave surface of TLR2 solenoid, not only induce NF-κB activation but also are associated with wild-type TLR2 and TLR6. These results suggest that the glycan at Asn442 and at least two N-linked glycans speculated to be exposed to the concave surface of TLR2 solenoid are involved in the recognition of ligands by TLR2 and/or in formation or maturation of a functional TLR2 receptor complex. |
Rights: | The definitive version is available at www.blackwell-synergy.com |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/30237 |
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)
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Submitter: 柴田 健一郎
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