Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870486 | FEBS Letters | 2014 | 7 Pages |
Abstract
Mannan binding lectin (MBL) functions as a pattern recognition molecule (PRM) which is able to initiate complement activation. Here, we characterize a previously unrecognized attribute of MBL as a double-stranded RNA (dsRNA) binding protein capable of modifying Toll like receptor 3 (TLR3) activation. MBL interacts with poly(I:C) and suppresses poly(I:C)-induced activation of TLR3 pathways and subsequent cytokine production. In addition, MBL binds to TLR3 directly. Surprisingly, disrupting the interaction between MBL and complement receptor 1 (CR1) or restraining the traffic of MBL to phagosome reversed the MBL limited TLR3 activation. We demonstrate the importance of MBL guided ligands intracellular localization, emphasizing the significance of understanding the dynamics of TLR agonists complexed with MBL or other PRMs inside the cell in immune defense.
Keywords
GlcNAcToll like receptor 3mDCsCRDPAMPTLRdsRNACLRMBLN-Acetyl-Glucosaminedouble-stranded RNApathogen-associated molecular patterninterferonIFNtumor necrosis factor αToll-like receptorcarbohydrate recognition domainDendritic cellMonocyte-derived dendritic cellsTNF-αMannan binding lectinMonocytepoly(I:C)Polyinosinic–polycytidylic acidComplement receptor
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Hongzhi Liu, Jia Zhou, Di Ma, Xiao Lu, Siqi Ming, Guiqiu Shan, Xiaoyong Zhang, Jinlin Hou, Zhengliang Chen, Daming Zuo,