Peptidoglycan recognition proteins （PGRP） play an important role in innate immunity in insects through the activation of the Imd pathway, which has been shown to be required in the antibacterial response in insects ...Peptidoglycan recognition proteins （PGRP） play an important role in innate immunity in insects through the activation of the Imd pathway, which has been shown to be required in the antibacterial response in insects and in the limitation of the number of Plasmodium berghei oocysts developing in mosquito midgut. The LCI gene of the PRGP family in Anopheles gambiae produces many products through alternative splicing. In this work, we demonstrate that PGRP-LC1a alone is sufficient to activate the Imd pathway in the A. gambiae L3-5 cell line through a combination of terminal or internal deletions, and RNA interference against endogenous PGRP-LC products. In the absence of endogenous PGRP-LC proteins, the integrity of the cytoplasmic domain is necessary for LCla function, while that of the extracellular domain is not. Moreover, the shorter the extracellular domain, the higher the activity for LC1 a. However, the removal of either the cytoplasmic or the extracellular PGRP-binding domain has little impact on the activity of LC 1 a in the presence of endogenous PGRP-LC proteins.展开更多
文摘Peptidoglycan recognition proteins （PGRP） play an important role in innate immunity in insects through the activation of the Imd pathway, which has been shown to be required in the antibacterial response in insects and in the limitation of the number of Plasmodium berghei oocysts developing in mosquito midgut. The LCI gene of the PRGP family in Anopheles gambiae produces many products through alternative splicing. In this work, we demonstrate that PGRP-LC1a alone is sufficient to activate the Imd pathway in the A. gambiae L3-5 cell line through a combination of terminal or internal deletions, and RNA interference against endogenous PGRP-LC products. In the absence of endogenous PGRP-LC proteins, the integrity of the cytoplasmic domain is necessary for LCla function, while that of the extracellular domain is not. Moreover, the shorter the extracellular domain, the higher the activity for LC1 a. However, the removal of either the cytoplasmic or the extracellular PGRP-binding domain has little impact on the activity of LC 1 a in the presence of endogenous PGRP-LC proteins.
