The Drosophila peptidoglycan-recognition protein LF interacts with peptidoglycan-recognition protein LC to downregulate the Imd pathway

被引:70
作者
Basbous, Nada [2 ]
Coste, Franck [2 ]
Leone, Philippe [1 ,3 ]
Vincentelli, Renaud [1 ,3 ]
Royet, Julien [3 ,4 ]
Kellenberger, Christine [2 ]
Roussel, Alain [1 ,2 ]
机构
[1] CNRS, UMR6098, F-13288 Marseille 9, France
[2] CNRS, UPR 4301, Ctr Biophys Mol, F-45071 Orleans, France
[3] Aix Marseille Univ, F-13288 Marseille 9, France
[4] CNRS, UMR6216, Inst Biol Dev Marseille Luminy, F-13288 Marseille 9, France
关键词
Drosophila; innate immunity; structural biology; IMMUNE-RESPONSE; PGRP-LC; BACTERIA;
D O I
10.1038/embor.2011.19
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The peptidoglycan (PGN)-recognition protein LF (PGRP-LF) is a specific negative regulator of the immune deficiency (Imd) pathway in Drosophila. We determine the crystal structure of the two PGRP domains constituting the ectodomain of PGRP-LF at 1.72 and 1.94 angstrom resolution. The structures show that the LFz and LFw domains do not have a PGN-docking groove that is found in other PGRP domains, and they cannot directly interact with PGN, as confirmed by biochemical-binding assays. By using surface plasmon resonance analysis, we show that the PGRP-LF ectodomain interacts with the PGRP-LCx ectodomain in the absence and presence of tracheal cytotoxin. Our results suggest a mechanism for downregulation of the Imd pathway on the basis of the competition between PRGP-LCa and PGRP-LF to bind to PGRP-LCx.
引用
收藏
页码:327 / 333
页数:7
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