Sensing and signaling during infection in Drosophila.

Most of the progress in dissecting the Drosophila antimicrobial response over the past decade has centered around intracellular signaling pathways in immune response tissues and expression of genes encoding antimicrobial peptide genes. The past few years, however, have witnessed significant advances in our understanding of the recognition of microbial invaders and subsequent activation of signaling cascades. In particular, the roles of peptidoglycan recognition proteins, which have known homologues in mammals, have been recognized and examined at the structural and functional levels.

[1]  K. Anderson,et al.  The antibacterial arm of the drosophila innate immune response requires an IkappaB kinase. , 2001, Genes & development.

[2]  B. Lemaître,et al.  Gram-negative Bacteria-binding Protein, a Pattern Recognition Receptor for Lipopolysaccharide and β-1,3-Glucan That Mediates the Signaling for the Induction of Innate Immune Genes in Drosophila melanogaster Cells* , 2000, The Journal of Biological Chemistry.

[3]  William M. Harley,et al.  Monomeric and polymeric gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway. , 2004, Immunity.

[4]  I. Wilson,et al.  Crystal structure of the Drosophila peptidoglycan recognition protein (PGRP)-SA at 1.56 A resolution. , 2004, Journal of molecular biology.

[5]  T. Aigaki,et al.  Overexpression of a pattern-recognition receptor, peptidoglycan-recognition protein-LE, activates imd/relish-mediated antibacterial defense and the prophenoloxidase cascade in Drosophila larvae , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[6]  B. Lemaître,et al.  The Drosophila immune system detects bacteria through specific peptidoglycan recognition , 2003, Nature Immunology.

[7]  D. Gubb,et al.  The Drosophila immune defense against gram-negative infection requires the death protein dFADD. , 2002, Immunity.

[8]  D. Hultmark,et al.  A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[9]  B. Lemaître,et al.  The Dorsoventral Regulatory Gene Cassette spätzle/Toll/cactus Controls the Potent Antifungal Response in Drosophila Adults , 1996, Cell.

[10]  Norbert Perrimon,et al.  Signaling role of hemocytes in Drosophila JAK/STAT-dependent response to septic injury. , 2003, Developmental cell.

[11]  M. Diaz-Meco,et al.  The Drosophila Atypical Protein Kinase C-Ref(2)P Complex Constitutes a Conserved Module for Signaling in the Toll Pathway , 2002, Molecular and Cellular Biology.

[12]  B. Lemaître,et al.  In Vivo RNA Interference Analysis Reveals an Unexpected Role for GNBP1 in the Defense against Gram-positive Bacterial Infection in Drosophila Adults* , 2004, Journal of Biological Chemistry.

[13]  S. Wasserman,et al.  Targeting of TAK1 by the NF-kappa B protein Relish regulates the JNK-mediated immune response in Drosophila. , 2004, Genes & development.

[14]  M. Belvin,et al.  Dual Activation of the Drosophila Toll Pathway by Two Pattern Recognition Receptors , 2003, Science.

[15]  M. Belvin,et al.  The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein , 2002, Nature.

[16]  S. Kurata,et al.  Peptidoglycan recognition protein (PGRP)‐LE and PGRP‐LC act synergistically in Drosophila immunity , 2004, The EMBO journal.

[17]  N. Gay,et al.  Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling , 2003, Nature Immunology.

[18]  P. Bulet,et al.  Critical evaluation of the role of the Toll‐like receptor 18‐Wheeler in the host defense of Drosophila , 2002, EMBO reports.

[19]  S. Wasserman,et al.  A heterotrimeric death domain complex in Toll signaling , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[20]  H. Steiner,et al.  A peptidoglycan recognition protein in innate immunity conserved from insects to humans. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[21]  M. Ashida,et al.  Purification of a Peptidoglycan Recognition Protein from Hemolymph of the Silkworm, Bombyx mori* , 1996, The Journal of Biological Chemistry.

[22]  J. Deisenhofer,et al.  A Drosophila Pattern Recognition Receptor Contains a Peptidoglycan Docking Groove and Unusual L,D-Carboxypeptidase Activity , 2004, PLoS biology.

[23]  M. Capovilla,et al.  Constitutive expression of a complement-like protein in toll and JAK gain-of-function mutants of Drosophila. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[24]  J. Hoffmann,et al.  Activation of Drosophila Toll During Fungal Infection by a Blood Serine Protease , 2002, Science.

[25]  D. Hultmark,et al.  Functional Diversity of the Drosophila PGRP-LC Gene Cluster in the Response to Lipopolysaccharide and Peptidoglycan* , 2003, Journal of Biological Chemistry.

[26]  R. Zhou,et al.  Role of Drosophila IKKγ in a Toll-independent antibacterial immune response , 2000, Nature Immunology.

[27]  B. Oh,et al.  Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster , 2003, Nature Immunology.

[28]  C. Janse,et al.  Complement-Like Protein TEP1 Is a Determinant of Vectorial Capacity in the Malaria Vector Anopheles gambiae , 2004, Cell.

[29]  J. Hoffmann,et al.  The immune response of Drosophila , 2003, Nature.

[30]  R. Dziarski.  Peptidoglycan recognition proteins (PGRPs). , 2004, Molecular immunology.

[31]  N. Perrimon,et al.  Sequential activation of signaling pathways during innate immune responses in Drosophila. , 2002, Developmental cell.

[32]  B. Lemaître,et al.  Inducible Expression of Double-Stranded RNA Reveals a Role for dFADD in the Regulation of the Antibacterial Response in Drosophila Adults , 2002, Current Biology.

[33]  T. Michel,et al.  Function of the drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria , 2004, Nature Immunology.

[34]  S. Tauszig-Delamasure,et al.  Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections , 2002, Nature Immunology.

[35]  T. Michel,et al.  Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein , 2001, Nature.

[36]  C. Nüsslein-Volhard,et al.  Krapfen/dMyd88 is required for the establishment of dorsoventral pattern in the Drosophila embryo , 2003, Mechanisms of Development.

[37]  Tom Maniatis,et al.  Caspase-mediated processing of the Drosophila NF-κB factor Relish , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[38]  P. Mellroth,et al.  A Scavenger Function for a DrosophilaPeptidoglycan Recognition Protein* , 2003, The Journal of Biological Chemistry.

[39]  M. Rämet,et al.  Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli , 2002, Nature.

[40]  M. Capovilla,et al.  Tissue and stage-specific expression of the Tolls in Drosophila embryos. , 2002, Gene expression patterns : GEP.

[41]  K. Anderson,et al.  Requirement for a Peptidoglycan Recognition Protein (PGRP) in Relish Activation and Antibacterial Immune Responses in Drosophila , 2002, Science.

[42]  M. Belvin,et al.  DmMyD88 controls dorsoventral patterning of the Drosophila embryo. , 2003 .