PGRP-LC and PGRP-LE have essential yet distinct functions in the drosophila immune response to monomeric DAP-type peptidoglycan
PGRP-LC and PGRP-LE have essential yet distinct functions in the drosophila immune response to monomeric DAP-type peptidoglycan
复制标题
DOI：
10.1038/ni1356
复制
发表时间：
2006-07-01
影响因子：
30.5
通讯作者：
Silverman, Neal
中科院分区：
文献类型：
--
作者：
Kaneko, Takashi;Yano, Tamaki;Silverman, Neal
果蝇完全依靠先天免疫反应来对抗微生物感染。由革兰氏阴性菌产生的含有二氨基海松酸的肽聚糖可被两种受体(PGRP-LC和PGRP-LE)识别，并通过IMD信号通路激活转录因子NF-kappa B的同系物。在这里，我们发现全长的PGRP-LE作为单体肽聚糖的细胞内受体，而只含有PGRP结构域的PGRP-LE版本像哺乳动物的CD14分子一样，在细胞外发挥功能，以增强PGRP-LC介导的肽聚糖在细胞表面的识别。PGRP-LC信号转导不需要与IMD信号蛋白相互作用。相反，PGRP-LC和PGRP-LE通过受体相互作用蛋白同型相互作用模体类基序发出信号。这些数据表明，像哺乳动物一样，果蝇利用细胞外和细胞内的受体进行先天免疫识别，这些受体具有保守的信号机制。
Drosophila rely entirely on an innate immune response to combat microbial infection. Diaminopimelic acid-containing peptidoglycan, produced by Gram-negative bacteria, is recognized by two receptors, PGRP-LC and PGRP-LE, and activates a homolog of transcription factor NF-kappa B through the Imd signaling pathway. Here we show that full-length PGRP-LE acted as an intracellular receptor for monomeric peptidoglycan, whereas a version of PGRP-LE containing only the PGRP domain functioned extracellularly, like the mammalian CD14 molecule, to enhance PGRP-LC-mediated peptidoglycan recognition on the cell surface. Interaction with the imd signaling protein was not required for PGRP-LC signaling. Instead, PGRP-LC and PGRP-LE signaled through a receptor-interacting protein homotypic interaction motif-like motif. These data demonstrate that like mammals, drosophila use both extracellular and intracellular receptors, which have conserved signaling mechanisms, for innate immune recognition.