Hemolymph-dependent and -independent responses in Drosophila immune tissue

被引:36
作者
Bettencourt, R
Asha, H
Dearolf, C
Ip, YT
机构
[1] Univ Massachusetts, Sch Med, Program Mol Med, Worcester, MA 01605 USA
[2] Univ Massachusetts, Sch Med, Dept Cell Biol, Worcester, MA 01605 USA
[3] Univ Massachusetts, Sch Med, Program Cell Dynam, Worcester, MA 01605 USA
[4] Massachusetts Gen Hosp, Dept Pediat, Boston, MA 02114 USA
关键词
innate immunity; hemolymph; Drosophila; NF-kappaB; dorsal;
D O I
10.1002/jcb.20123
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
Insects possess an antimicrobial defense response that is similar to the mammalian innate immune response. The innate immune system is designed to recognize conserved components of microorganisms called pathogen associated molecular patterns (PAMPs). How host receptors detect PAMPs and transmit the signals to mount the immune response is being elucidated. Using GFP-Dorsal, -Dif, and -Relish reporter proteins in ex vivo assays, we demonstrate that Drosophila fat bodies, a major immune tissue, have both hemolymph-dependent and -independent responses. Microbial preparations such as lipoteichoic acid (LTA) and peptidoglycan (PGN) can stimulate some responses from dissected and rinsed larval fat bodies. Therefore, at least some aspects of recognition can occur on fat body cell surfaces, bypassing the requirement of hemolymph. Our results also show that supernatants from bacterial cultures can stimulate the nuclear translocation of Dorsal in dissected fat bodies, but this stimulation is strictly hemolymph-dependent. Various biochemical assays suggest that the factors from bacterial supernatants that stimulate the hemolymph-dependent nuclear translocation are likely made up of proteins. We further show that Dorsal mutant larvae have much lower phenoloxidase activity, consistent with a more important role of Dorsal in innate immunity than previously shown. (C) 2004 Wiley-Liss, Inc.
引用
收藏
页码:849 / 863
页数:15
相关论文
共 45 条
[1]   Toll signaling pathways in the innate immune response [J].
Anderson, KV .
CURRENT OPINION IN IMMUNOLOGY, 2000, 12 (01) :13-19
[2]  
Asha H, 2003, GENETICS, V163, P203
[3]   NF-kappa B: Ten years after [J].
Baeuerle, PA ;
Baltimore, D .
CELL, 1996, 87 (01) :13-20
[4]  
BRAND AH, 1993, DEVELOPMENT, V118, P401
[5]   Requirement for a peptidoglycan recognition protein (PGRP) in relish activation and antibacterial immune responses in Drosophila [J].
Choe, KM ;
Werner, T ;
Stöven, S ;
Hultmark, D ;
Anderson, KV .
SCIENCE, 2002, 296 (5566) :359-362
[6]   Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex - Transfer from CD14 to TLR4 and MD-2 [J].
Correia, JD ;
Soldau, K ;
Christen, U ;
Tobias, PS ;
Ulevitch, RJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (24) :21129-21135
[7]   Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis [J].
Georgel, P ;
Naitza, S ;
Kappler, C ;
Ferrandon, D ;
Zachary, D ;
Swimmer, C ;
Kopczynski, C ;
Duyk, G ;
Reichart, JM ;
Hoffmann, JA .
DEVELOPMENTAL CELL, 2001, 1 (04) :503-514
[8]   NF-κB and rel proteins:: Evolutionarily conserved mediators of immune responses [J].
Ghosh, S ;
May, MJ ;
Kopp, EB .
ANNUAL REVIEW OF IMMUNOLOGY, 1998, 16 :225-260
[9]  
GILMORE TD, 2003, NATURE ENCY LIFE SCI
[10]   The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein [J].
Gottar, M ;
Gobert, V ;
Michel, T ;
Belvin, M ;
Duyk, G ;
Hoffmann, JA ;
Ferrandon, D ;
Royet, J .
NATURE, 2002, 416 (6881) :640-644