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中文摘要：
脂多糖（LPS）的识别和信号转导是宿主发生防御反应的关键,Toll样受体4（TLR4）与髓样分化蛋白-2（MD-2）形成复合物在LPS的识别及其信号转导中发挥了重要作用.研究TLR4与MD-2结合的功能结构域,对于深入了解LPS信号转导机制及其内毒素休克的防治具有重要意义.运用基于强度的三通道荧光共振能量转移技术（FRET）及基因突变和转染技术,研究了活细胞TLR4与MD-2作用的结构域.结果表明：N端Glu24～Met41缺失使TLR4与MD-2结合能力明显下降;LPS刺激后TLR4聚合迅速增加,而缺失Glu24～Met41的TLR4不能聚合.上述结果提示,TLR4的Glu24～Met41不仅是结合MD-2的区域,并且还参与了LPS刺激后TLR4的聚合作用.
英文摘要：
TLR4-MD-2 complex plays a key role in LPS recognition and its signal transduction.These steps are the vital elements of the host＇s defensive reaction.Studying the functional domain of TLR4 and MD-2 is very important to further understand the mechanism of LPS signal transduction.It was studied the interaction domain of TLR4 and MD-2 in living cells based on gene mutation,gene transfection and fluorescence resonance energy tramsfer（FRET） which is considered as one of the best methods used for intracellular protein-protein interaction study.CY-15P which was fused by CFP and YFP through 15 neutral amino acids was used as positive control,while co-expressed CFP and YFP proteins were used as negative control.The results showed that the ability of TLR4 binding to MD-2 decreased dramatically after the deletion of Glu 24 ～Met 41 in N terminal of TLR4.Aggregation of TLR4 to LPS stimulation was observed,however,TLR4 without the Glu 24 ～Met 41 mutation did not aggregate.All these results indicated that TLR4 Glu 24 ～Met 41 might be the interaction domain of TLR4 binding to MD-2 and participate in the aggregation effect of TLR4 upon LPS stimulation.
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