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RISS 인기검색어
- 검색키워드
- 저자 : Xue Hua Nan (검색결과 2 건)
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Mechanism of pattern recognition by TLR2-TLR6 heterodimer
Nan, Xue Hua 충남대학교 대학원 2010 국내박사
TLR2 initiates potent immune responses by recognizing diacylated and triacylated lipopeptides. Its ligand specificity is controlled by whether it heterodimerizes with TLR1 or TLR6. In present study, we found three major factors contribute to the ligand specificity of TLR2-TLR1/6 heterodimers. First, the lipid channel of TLR6 has two phenylalanines, which block the lipid channel for amide bound lipid chain of triacylated lipopeptides. Simultaneous mutation of these phenylalanines made TLR2-TLR6 fully responsive not only to diacylated but also to triacylated lipopeptides. Second, through the alanine mutation exprimens of human TLR6, Asn314, Phe319, Tyr325, Thr326, Cys348, Gln362, Asp367, Phe370, Cys373 and Lys390 are found to be important residues in the ligand induced activation of TLR2/TLR6 heterodimerization. Furthermore, PE-DTPA, a phosphatidylethanolamine derivative, forms a stable complex with TLR2, but it cannot induce downstream signaling. We found that TLR2 cannot form heterodimers with TLR1 and TLR6 by binding PE-DTPA. This data demonstrates that two lipid chains are required but not enough for TLR2 activation. Collectively, a precise interaction pattern of the head group of ligand is essential for a robust immune response by TLR2 heterodimers.
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