Imler Jean-Luc
Overview of Drosophila immunity: a historical perspective Journal Article
In: Developmental and Comparative Immunology, vol. 42, no. 1, pp. 3–15, 2014, ISSN: 1879-0089.
Abstract | Links | BibTeX | Tags: Allergy and Immunology, Animal, Animals, Antimicrobial Cationic Peptides, Antimicrobial peptides, history, Humans, IMD pathway, imler, Immunity, Innate, innate immunity, M3i, Models, Pattern recognition receptors, Signal Transduction, Toll-Like Receptors
@article{imler_overview_2014,
title = {Overview of Drosophila immunity: a historical perspective},
author = {Jean-Luc Imler},
doi = {10.1016/j.dci.2013.08.018},
issn = {1879-0089},
year = {2014},
date = {2014-01-01},
journal = {Developmental and Comparative Immunology},
volume = {42},
number = {1},
pages = {3--15},
abstract = {The functional analysis of genes from the model organism Drosophila melanogaster has provided invaluable information for many cellular and developmental or physiological processes, including immunity. The best-understood aspect of Drosophila immunity is the inducible humoral response, first recognized in 1972. This pioneering work led to a remarkable series of findings over the next 30 years, ranging from the identification and characterization of the antimicrobial peptides produced, to the deciphering of the signalling pathways activating the genes that encode them and, ultimately, to the discovery of the receptors sensing infection. These studies on an insect model coincided with a revival of the field of innate immunity, and had an unanticipated impact on the biomedical field.},
keywords = {Allergy and Immunology, Animal, Animals, Antimicrobial Cationic Peptides, Antimicrobial peptides, history, Humans, IMD pathway, imler, Immunity, Innate, innate immunity, M3i, Models, Pattern recognition receptors, Signal Transduction, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
Haller Samantha, Limmer Stefanie, Ferrandon Dominique
Assessing Pseudomonas virulence with a nonmammalian host: Drosophila melanogaster Journal Article
In: Methods Mol. Biol., vol. 1149, pp. 723–740, 2014, ISSN: 1940-6029.
Abstract | Links | BibTeX | Tags: Animal, Animals, Antimicrobial Cationic Peptides, Biological Assay, Colony Count, Disease Models, ferrandon, Hemolymph, Host-Pathogen Interactions, M3i, Mammals, Microbial, Pseudomonas aeruginosa, Pseudomonas Infections, Reverse Transcriptase Polymerase Chain Reaction, Virulence
@article{haller_assessing_2014b,
title = {Assessing Pseudomonas virulence with a nonmammalian host: Drosophila melanogaster},
author = {Samantha Haller and Stefanie Limmer and Dominique Ferrandon},
doi = {10.1007/978-1-4939-0473-0_56},
issn = {1940-6029},
year = {2014},
date = {2014-01-01},
journal = {Methods Mol. Biol.},
volume = {1149},
pages = {723--740},
abstract = {Drosophila melanogaster flies represent an interesting model to study host-pathogen interactions as: (1) they are cheap and easy to raise rapidly and do not bring up ethical issues, (2) available genetic tools are highly sophisticated, for instance allowing tissue-specific alteration of gene expression, e.g., of immune genes, (3) they have a relatively complex organization, with distinct digestive tract and body cavity in which local or systemic infections, respectively, take place, (4) a medium throughput can be achieved in genetic screens, for instance looking for Pseudomonas aeruginosa mutants with altered virulence. We present here the techniques used to investigate host-pathogen relationships, namely the two major models of infections as well as the relevant parameters used to monitor the infection (survival, bacterial titer, induction of host immune response).},
keywords = {Animal, Animals, Antimicrobial Cationic Peptides, Biological Assay, Colony Count, Disease Models, ferrandon, Hemolymph, Host-Pathogen Interactions, M3i, Mammals, Microbial, Pseudomonas aeruginosa, Pseudomonas Infections, Reverse Transcriptase Polymerase Chain Reaction, Virulence},
pubstate = {published},
tppubtype = {article}
}
Baron Olga Lucia, van West Pieter, Industri Benoit, Ponchet Michel, Dubreuil Géraldine, Gourbal Benjamin, Reichhart Jean-Marc, Coustau Christine
Parental transfer of the antimicrobial protein LBP/BPI protects Biomphalaria glabrata eggs against oomycete infections Journal Article
In: PLoS Pathog., vol. 9, no. 12, pp. e1003792, 2013, ISSN: 1553-7374.
Abstract | Links | BibTeX | Tags: Acute-Phase Proteins, Animals, Antimicrobial Cationic Peptides, Biomphalaria, Blood Proteins, Carrier Proteins, Cell Membrane, Cell Membrane Permeability, Cloning, Escherichia coli, Female, Immunity, infection, M3i, Maternally-Acquired, Membrane Glycoproteins, Microbial Sensitivity Tests, Molecular, Oomycetes, Recombinant Proteins, reichhart, Zygote
@article{baron_parental_2013,
title = {Parental transfer of the antimicrobial protein LBP/BPI protects Biomphalaria glabrata eggs against oomycete infections},
author = {Olga Lucia Baron and Pieter van West and Benoit Industri and Michel Ponchet and Géraldine Dubreuil and Benjamin Gourbal and Jean-Marc Reichhart and Christine Coustau},
doi = {10.1371/journal.ppat.1003792},
issn = {1553-7374},
year = {2013},
date = {2013-01-01},
journal = {PLoS Pathog.},
volume = {9},
number = {12},
pages = {e1003792},
abstract = {Vertebrate females transfer antibodies via the placenta, colostrum and milk or via the egg yolk to protect their immunologically immature offspring against pathogens. This evolutionarily important transfer of immunity is poorly documented in invertebrates and basic questions remain regarding the nature and extent of parental protection of offspring. In this study, we show that a lipopolysaccharide binding protein/bactericidal permeability increasing protein family member from the invertebrate Biomphalaria glabrata (BgLBP/BPI1) is massively loaded into the eggs of this freshwater snail. Native and recombinant proteins displayed conserved LPS-binding, antibacterial and membrane permeabilizing activities. A broad screening of various pathogens revealed a previously unknown biocidal activity of the protein against pathogenic water molds (oomycetes), which is conserved in human BPI. RNAi-dependent silencing of LBP/BPI in the parent snails resulted in a significant reduction of reproductive success and extensive death of eggs through oomycete infections. This work provides the first functional evidence that a LBP/BPI is involved in the parental immune protection of invertebrate offspring and reveals a novel and conserved biocidal activity for LBP/BPI family members.},
keywords = {Acute-Phase Proteins, Animals, Antimicrobial Cationic Peptides, Biomphalaria, Blood Proteins, Carrier Proteins, Cell Membrane, Cell Membrane Permeability, Cloning, Escherichia coli, Female, Immunity, infection, M3i, Maternally-Acquired, Membrane Glycoproteins, Microbial Sensitivity Tests, Molecular, Oomycetes, Recombinant Proteins, reichhart, Zygote},
pubstate = {published},
tppubtype = {article}
}
Nehme Nadine T, Quintin Jessica, Cho Ju Hyun, Lee Janice, Lafarge Marie-Céline, Kocks Christine, Ferrandon Dominique
Relative roles of the cellular and humoral responses in the Drosophila host defense against three gram-positive bacterial infections Journal Article
In: PLoS ONE, vol. 6, no. 3, pp. e14743, 2011, ISSN: 1932-6203.
Abstract | Links | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, Carrier Proteins, Cell Surface, Cellular, Enterococcus faecalis, ferrandon, Gram-Positive Bacteria, Gram-Positive Bacterial Infections, Host-Pathogen Interactions, Humoral, Immunity, Innate, M3i, Micrococcus luteus, Opsonin Proteins, Phagocytosis, Receptors, Signal Transduction, Solubility, Staphylococcus aureus
@article{nehme_relative_2011b,
title = {Relative roles of the cellular and humoral responses in the Drosophila host defense against three gram-positive bacterial infections},
author = {Nadine T Nehme and Jessica Quintin and Ju Hyun Cho and Janice Lee and Marie-Céline Lafarge and Christine Kocks and Dominique Ferrandon},
doi = {10.1371/journal.pone.0014743},
issn = {1932-6203},
year = {2011},
date = {2011-01-01},
journal = {PLoS ONE},
volume = {6},
number = {3},
pages = {e14743},
abstract = {BACKGROUND: Two NF-kappaB signaling pathways, Toll and immune deficiency (imd), are required for survival to bacterial infections in Drosophila. In response to septic injury, these pathways mediate rapid transcriptional activation of distinct sets of effector molecules, including antimicrobial peptides, which are important components of a humoral defense response. However, it is less clear to what extent macrophage-like hemocytes contribute to host defense. METHODOLOGY/PRINCIPAL FINDINGS: In order to dissect the relative importance of humoral and cellular defenses after septic injury with three different gram-positive bacteria (Micrococcus luteus, Enterococcus faecalis, Staphylococcus aureus), we used latex bead pre-injection to ablate macrophage function in flies wildtype or mutant for various Toll and imd pathway components. We found that in all three infection models a compromised phagocytic system impaired fly survival--independently of concomitant Toll or imd pathway activation. Our data failed to confirm a role of the PGRP-SA and GNBP1 Pattern Recognition Receptors for phagocytosis of S. aureus. The Drosophila scavenger receptor Eater mediates the phagocytosis by hemocytes or S2 cells of E. faecalis and S. aureus, but not of M. luteus. In the case of M. luteus and E. faecalis, but not S. aureus, decreased survival due to defective phagocytosis could be compensated for by genetically enhancing the humoral immune response. CONCLUSIONS/SIGNIFICANCE: Our results underscore the fundamental importance of both cellular and humoral mechanisms in Drosophila immunity and shed light on the balance between these two arms of host defense depending on the invading pathogen.},
keywords = {Animals, Antimicrobial Cationic Peptides, Carrier Proteins, Cell Surface, Cellular, Enterococcus faecalis, ferrandon, Gram-Positive Bacteria, Gram-Positive Bacterial Infections, Host-Pathogen Interactions, Humoral, Immunity, Innate, M3i, Micrococcus luteus, Opsonin Proteins, Phagocytosis, Receptors, Signal Transduction, Solubility, Staphylococcus aureus},
pubstate = {published},
tppubtype = {article}
}
Bischoff Vincent, Vignal Cécile, Duvic Bernard, Boneca Ivo G, Hoffmann Jules A, Royet Julien
Downregulation of the Drosophila immune response by peptidoglycan-recognition proteins SC1 and SC2 Journal Article
In: PLoS Pathog., vol. 2, no. 2, pp. e14, 2006, ISSN: 1553-7374.
Abstract | Links | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, bacteria, Carrier Proteins, Down-Regulation, hoffmann, Larva, M3i, RNA Interference, Signal Transduction
@article{bischoff_downregulation_2006,
title = {Downregulation of the Drosophila immune response by peptidoglycan-recognition proteins SC1 and SC2},
author = {Vincent Bischoff and Cécile Vignal and Bernard Duvic and Ivo G Boneca and Jules A Hoffmann and Julien Royet},
doi = {10.1371/journal.ppat.0020014},
issn = {1553-7374},
year = {2006},
date = {2006-02-01},
journal = {PLoS Pathog.},
volume = {2},
number = {2},
pages = {e14},
abstract = {Peptidoglycan-recognition proteins (PGRPs) are evolutionarily conserved molecules that are structurally related to bacterial amidases. Several Drosophila PGRPs have lost this enzymatic activity and serve as microbe sensors through peptidoglycan recognition. Other PGRP family members, such as Drosophila PGRP-SC1 or mammalian PGRP-L, have conserved the amidase function and are able to cleave peptidoglycan in vitro. However, the contribution of these amidase PGRPs to host defense in vivo has remained elusive so far. Using an RNA-interference approach, we addressed the function of two PGRPs with amidase activity in the Drosophila immune response. We observed that PGRP-SC1/2-depleted flies present a specific over-activation of the IMD (immune deficiency) signaling pathway after bacterial challenge. Our data suggest that these proteins act in the larval gut to prevent activation of this pathway following bacterial ingestion. We further show that a strict control of IMD-pathway activation is essential to prevent bacteria-induced developmental defects and larval death.},
keywords = {Animals, Antimicrobial Cationic Peptides, bacteria, Carrier Proteins, Down-Regulation, hoffmann, Larva, M3i, RNA Interference, Signal Transduction},
pubstate = {published},
tppubtype = {article}
}
Royet Julien, Reichhart Jean-Marc, Hoffmann Jules A
Sensing and signaling during infection in Drosophila Journal Article
In: Curr. Opin. Immunol., vol. 17, no. 1, pp. 11–17, 2005, ISSN: 0952-7915.
Abstract | Links | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, Bacterial Infections, Gene Expression Regulation, Genome, hoffmann, Immunity, Innate, M3i, reichhart, Signal Transduction
@article{royet_sensing_2005,
title = {Sensing and signaling during infection in Drosophila},
author = {Julien Royet and Jean-Marc Reichhart and Jules A Hoffmann},
doi = {10.1016/j.coi.2004.12.002},
issn = {0952-7915},
year = {2005},
date = {2005-02-01},
journal = {Curr. Opin. Immunol.},
volume = {17},
number = {1},
pages = {11--17},
abstract = {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.},
keywords = {Animals, Antimicrobial Cationic Peptides, Bacterial Infections, Gene Expression Regulation, Genome, hoffmann, Immunity, Innate, M3i, reichhart, Signal Transduction},
pubstate = {published},
tppubtype = {article}
}
Imler Jean-Luc, Bulet Philippe
Antimicrobial peptides in Drosophila: structures, activities and gene regulation Journal Article
In: Chemical Immunology and Allergy, vol. 86, pp. 1–21, 2005, ISSN: 1660-2242.
Abstract | Links | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, Defensins, Gene Expression Regulation, Genes, Glycopeptides, imler, Immunity, Innate, Insect, Insect Proteins, M3i, Molecular Structure, Signal Transduction
@article{imler_antimicrobial_2005,
title = {Antimicrobial peptides in Drosophila: structures, activities and gene regulation},
author = {Jean-Luc Imler and Philippe Bulet},
doi = {10.1159/000086648},
issn = {1660-2242},
year = {2005},
date = {2005-01-01},
journal = {Chemical Immunology and Allergy},
volume = {86},
pages = {1--21},
abstract = {The production of antimicrobial peptides (AMPs) is an important aspect of host-defence in multicellular organisms. Biochemical analysis of the hemolymph of the fruit-fly Drosophila melanogaster and other Diptera has led to the discovery of eight classes of AMPs. These peptides can be grouped into three families based on their main biological targets, gram-positive bacteria (defensin), gram-negative bacteria (cecropins, drosocin, attacins, diptericin, MPAC), or fungi (drosomycin, metchnikowin). Drosophila AMPs are synthesized by the fat body in response to infection, and secreted into the blood. Most of them can also be induced in surface epithelia in a tissue-specific manner. Finally, some of them are constitutively expressed in defined tissues, such as the salivary glands or the reproductive tract. We review here the structures and activities of these AMPs, as well as the signalling cascades, which lead to their induction upon detection of infectious non-self.},
keywords = {Animals, Antimicrobial Cationic Peptides, Defensins, Gene Expression Regulation, Genes, Glycopeptides, imler, Immunity, Innate, Insect, Insect Proteins, M3i, Molecular Structure, Signal Transduction},
pubstate = {published},
tppubtype = {article}
}
Thouzeau Cécile, Maho Yvon Le, Froget Guillaume, Sabatier Laurence, Bohec Céline Le, Hoffmann Jules A, Bulet Philippe
Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus Journal Article
In: J. Biol. Chem., vol. 278, no. 51, pp. 51053–51058, 2003, ISSN: 0021-9258.
Abstract | Links | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, bacteria, beta-Defensins, Birds, Feeding Behavior, Fungi, Gastrointestinal Contents, hoffmann, M3i, Male, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Isoforms, Sequence Alignment, Spectrometry
@article{thouzeau_spheniscins_2003,
title = {Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus},
author = {Cécile Thouzeau and Yvon Le Maho and Guillaume Froget and Laurence Sabatier and Céline Le Bohec and Jules A Hoffmann and Philippe Bulet},
doi = {10.1074/jbc.M306839200},
issn = {0021-9258},
year = {2003},
date = {2003-12-01},
journal = {J. Biol. Chem.},
volume = {278},
number = {51},
pages = {51053--51058},
abstract = {During the last part of egg incubation in king penguins, the male can preserve undigested food in the stomach for several weeks. This ensures survival of the newly hatched chick, in cases where the return of the foraging female from the sea is delayed. In accordance with the characterization of stress-induced bacteria, we demonstrate the occurrence of strong antimicrobial activities in preserved stomach contents. We isolated and fully characterized two isoforms of a novel 38-residue antimicrobial peptide (AMP), spheniscin, belonging to the beta-defensin subfamily. Spheniscin concentration was found to strongly increase during the period of food storage. Using a synthetic version of one of two spheniscin isoforms, we established that this peptide has a broad activity spectrum, affecting the growth of both pathogenic bacteria and fungi. Altogether, our data suggest that spheniscins and other, not yet identified, antimicrobial substances may play a role in the long term preservation of stored food in the stomach of king penguins.},
keywords = {Animals, Antimicrobial Cationic Peptides, bacteria, beta-Defensins, Birds, Feeding Behavior, Fungi, Gastrointestinal Contents, hoffmann, M3i, Male, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Isoforms, Sequence Alignment, Spectrometry},
pubstate = {published},
tppubtype = {article}
}
Ligoxygakis Petros, Bulet Philippe, Reichhart Jean-Marc
Critical evaluation of the role of the Toll-like receptor 18-Wheeler in the host defense of Drosophila Journal Article
In: EMBO Rep., vol. 3, no. 7, pp. 666–673, 2002, ISSN: 1469-221X.
Abstract | Links | BibTeX | Tags: Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Cell Adhesion Molecules, Fat Body, Gene Expression Regulation, Genes, Immunohistochemistry, Immunologic, Insect, Insect Proteins, Larva, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Membrane Proteins, Receptors, reichhart, Reporter, Spectrometry, Transgenes
@article{ligoxygakis_critical_2002,
title = {Critical evaluation of the role of the Toll-like receptor 18-Wheeler in the host defense of Drosophila},
author = {Petros Ligoxygakis and Philippe Bulet and Jean-Marc Reichhart},
doi = {10.1093/embo-reports/kvf130},
issn = {1469-221X},
year = {2002},
date = {2002-01-01},
journal = {EMBO Rep.},
volume = {3},
number = {7},
pages = {666--673},
abstract = {Essential aspects of innate immune responses to microbial infections appear to be conserved between insects and mammals. In particular, in both groups, transmembrane receptors of the Toll superfamily play a crucial role in activating immune defenses. The Drosophila Toll family member 18-Wheeler had been proposed to sense Gram-negative infection and direct selective expression of peptides active against Gram-negative bacteria. Here we re-examine the role of 18-Wheeler and show that in adults it is dispensable for immune responses. In larvae, 18wheeler is required for normal fat body development, and in mutant larvae induction of all antimicrobial peptide genes, and not only of those directed against Gram-negative bacteria, is compromised. 18-Wheeler does not qualify as a pattern recognition receptor of Gram-negative bacteria.},
keywords = {Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Cell Adhesion Molecules, Fat Body, Gene Expression Regulation, Genes, Immunohistochemistry, Immunologic, Insect, Insect Proteins, Larva, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Membrane Proteins, Receptors, reichhart, Reporter, Spectrometry, Transgenes},
pubstate = {published},
tppubtype = {article}
}
Tauszig-Delamasure Servane, Bilak Hana, Capovilla Maria, Hoffmann Jules A, Imler Jean-Luc
Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections Journal Article
In: Nature Immunology, vol. 3, no. 1, pp. 91–97, 2002, ISSN: 1529-2908.
Abstract | Links | BibTeX | Tags: Adaptor Proteins, Amino Acid, Animals, Antigens, Antimicrobial Cationic Peptides, Cell Surface, Chromosome Mapping, Differentiation, Disease Susceptibility, Enterococcus faecalis, Epistasis, Escherichia coli, Female, Gene Expression Regulation, Genes, Genetic, Genetically Modified, Gram-Negative Bacteria, hoffmann, Hypocreales, imler, Immunologic, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Micrococcus luteus, Myeloid Differentiation Factor 88, Protein Structure, Protein-Serine-Threonine Kinases, Receptors, Recombinant Fusion Proteins, Sequence Alignment, Sequence Homology, Signal Transducing, Tertiary, Toll-Like Receptors, Transfection
@article{tauszig-delamasure_drosophila_2002,
title = {Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections},
author = {Servane Tauszig-Delamasure and Hana Bilak and Maria Capovilla and Jules A Hoffmann and Jean-Luc Imler},
doi = {10.1038/ni747},
issn = {1529-2908},
year = {2002},
date = {2002-01-01},
journal = {Nature Immunology},
volume = {3},
number = {1},
pages = {91--97},
abstract = {We report here the identification and functional characterization of DmMyD88, a gene encoding the Drosophila homolog of mammalian MyD88. DmMyD88 combines a Toll-IL-1R homology (TIR) domain and a death domain. Overexpression of DmMyD88 was sufficient to induce expression of the antifungal peptide Drosomycin, and induction of Drosomycin was markedly reduced in DmMyD88-mutant flies. DmMyD88 interacted with Toll through its TIR domain and required the death domain proteins Tube and Pelle to activate expression of Drs, which encodes Drosomycin. DmMyD88-mutant flies were highly susceptible to infection by fungi and Gram-positive bacteria, but resisted Gram-negative bacterial infection much as did wild-type flies. Phenotypic comparison of DmMyD88-mutant flies and MyD88-deficient mice showed essential differences in the control of Gram-negative infection in insects and mammals.},
keywords = {Adaptor Proteins, Amino Acid, Animals, Antigens, Antimicrobial Cationic Peptides, Cell Surface, Chromosome Mapping, Differentiation, Disease Susceptibility, Enterococcus faecalis, Epistasis, Escherichia coli, Female, Gene Expression Regulation, Genes, Genetic, Genetically Modified, Gram-Negative Bacteria, hoffmann, Hypocreales, imler, Immunologic, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Micrococcus luteus, Myeloid Differentiation Factor 88, Protein Structure, Protein-Serine-Threonine Kinases, Receptors, Recombinant Fusion Proteins, Sequence Alignment, Sequence Homology, Signal Transducing, Tertiary, Toll-Like Receptors, Transfection},
pubstate = {published},
tppubtype = {article}
}
Boulanger Nathalie, Ehret-Sabatier Laurence, Brun R, Zachary Daniel, Bulet Philippe, Imler Jean-Luc
Immune response of Drosophila melanogaster to infection with the flagellate parasite Crithidia spp Journal Article
In: Insect Biochemistry and Molecular Biology, vol. 31, no. 2, pp. 129–137, 2001, ISSN: 0965-1748.
Abstract | BibTeX | Tags: Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Crithidia, Defensins, Gene Expression, Glycopeptides, Hemocytes, imler, Insect Proteins, M3i, Phagocytosis
@article{boulanger_immune_2001,
title = {Immune response of Drosophila melanogaster to infection with the flagellate parasite Crithidia spp},
author = {Nathalie Boulanger and Laurence Ehret-Sabatier and R Brun and Daniel Zachary and Philippe Bulet and Jean-Luc Imler},
issn = {0965-1748},
year = {2001},
date = {2001-02-01},
journal = {Insect Biochemistry and Molecular Biology},
volume = {31},
number = {2},
pages = {129--137},
abstract = {Insects are able to recognize invading microorganisms and to mount an immune response to bacterial and fungal infections. Recently, the fruitfly Drosophila melanogaster has emerged as a promising invertebrate model to investigate innate immunity because of its well-characterized genetics. Insects are also vectors of numerous parasites which can trigger an immune response. We have investigated the interaction of Drosophila melanogaster with the flagellate protozoan Crithidia spp. We show that a per os parasitic infection triggers the synthesis of several antimicrobial peptides. By reverse phase HPLC and mass spectrometry, peptides were shown to be present in the hemolymph and not in the gut tissue, suggesting the presence of immune messengers between the site of the infection, namely the gut, and the fat body, the main site of synthesis for antimicrobial peptides. Interestingly, we have identified one molecule which is specifically induced in the hemolymph after infection with Crithidia, but not with bacteria, suggesting that Drosophila can discriminate between pathogens. When flagellates were injected into the hemolymph, a low synthesis of antimicrobial peptides was observed together with phagocytosis of parasites by circulating hemocytes. The data presented here suggest that Drosophila-Crithidia spp. represents an interesting model to study host defense against protozoan parasites.},
keywords = {Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Crithidia, Defensins, Gene Expression, Glycopeptides, Hemocytes, imler, Insect Proteins, M3i, Phagocytosis},
pubstate = {published},
tppubtype = {article}
}
Levashina Elena A, Langley E, Green C, Gubb David, Ashburner M, Hoffmann Jules A, Reichhart Jean-Marc
Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila Journal Article
In: Science, vol. 285, no. 5435, pp. 1917–1919, 1999, ISSN: 0036-8075.
Abstract | BibTeX | Tags: Animals, Antifungal Agents, Antimicrobial Cationic Peptides, Body Patterning, Cell Surface, Escherichia coli, Genes, Hemolymph, hoffmann, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Micrococcus luteus, Mutagenesis, Peptides, Receptors, Recombinant Fusion Proteins, reichhart, Serine Proteinase Inhibitors, Serpins, Signal Transduction, Toll-Like Receptors, Up-Regulation
@article{levashina_constitutive_1999,
title = {Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila},
author = {Elena A Levashina and E Langley and C Green and David Gubb and M Ashburner and Jules A Hoffmann and Jean-Marc Reichhart},
issn = {0036-8075},
year = {1999},
date = {1999-09-01},
journal = {Science},
volume = {285},
number = {5435},
pages = {1917--1919},
abstract = {The antifungal defense of Drosophila is controlled by the spaetzle/Toll/cactus gene cassette. Here, a loss-of-function mutation in the gene encoding a blood serine protease inhibitor, Spn43Ac, was shown to lead to constitutive expression of the antifungal peptide drosomycin, and this effect was mediated by the spaetzle and Toll gene products. Spaetzle was cleaved by proteolytic enzymes to its active ligand form shortly after immune challenge, and cleaved Spaetzle was constitutively present in Spn43Ac-deficient flies. Hence, Spn43Ac negatively regulates the Toll signaling pathway, and Toll does not function as a pattern recognition receptor in the Drosophila host defense.},
keywords = {Animals, Antifungal Agents, Antimicrobial Cationic Peptides, Body Patterning, Cell Surface, Escherichia coli, Genes, Hemolymph, hoffmann, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Micrococcus luteus, Mutagenesis, Peptides, Receptors, Recombinant Fusion Proteins, reichhart, Serine Proteinase Inhibitors, Serpins, Signal Transduction, Toll-Like Receptors, Up-Regulation},
pubstate = {published},
tppubtype = {article}
}
Levashina Elena A, Ohresser S, Lemaitre Bruno, Imler Jean-Luc
Two distinct pathways can control expression of the gene encoding the Drosophila antimicrobial peptide metchnikowin Journal Article
In: Journal of Molecular Biology, vol. 278, no. 3, pp. 515–527, 1998, ISSN: 0022-2836.
Abstract | Links | BibTeX | Tags: Animals, Anti-Infective Agents, Antimicrobial Cationic Peptides, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, Glycopeptides, imler, Insect, Insect Proteins, Larva, M3i, Molecular, Mutation, Peptides, Promoter Regions, Recombinant Fusion Proteins, Reporter, Restriction Mapping, Transcription
@article{levashina_two_1998,
title = {Two distinct pathways can control expression of the gene encoding the Drosophila antimicrobial peptide metchnikowin},
author = {Elena A Levashina and S Ohresser and Bruno Lemaitre and Jean-Luc Imler},
doi = {10.1006/jmbi.1998.1705},
issn = {0022-2836},
year = {1998},
date = {1998-01-01},
journal = {Journal of Molecular Biology},
volume = {278},
number = {3},
pages = {515--527},
abstract = {Metchnikowin is a recently discovered proline-rich peptide from Drosophila with antibacterial and antifungal properties. Like most other antimicrobial peptides from insects, its expression is immune-inducible. Here we present evidence that induction of metchnikowin gene expression can be mediated either by the TOLL pathway or by the imd gene product. We show that the gene remains inducible in Toll-deficient mutants, in which the antifungal response is blocked, as well as in imd mutants, which fail to mount an antibacterial response. However, in Toll-deficient;imd double mutants, metchnikowin gene expression can no longer be detected after immune challenge. Our results suggest that expression of this peptide with dual activity can be triggered by signals generated by either bacterial or fungal infection. Cloning of the metchnikowin gene revealed the presence in the 5' flanking region of several putative cis-regulatory motifs characterized in the promoters of insect immune genes: namely, Rel sites, GATA motifs, interferon consensus response elements and NF-IL6 response elements. Establishment of transgenic fly lines in which the GFP reporter gene was placed under the control of 1.5 kb of metchnikowin gene upstream sequences indicates that this fragment is able to confer full immune inducibility and tissue specificity of expression on the transgene.},
keywords = {Animals, Anti-Infective Agents, Antimicrobial Cationic Peptides, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, Glycopeptides, imler, Insect, Insect Proteins, Larva, M3i, Molecular, Mutation, Peptides, Promoter Regions, Recombinant Fusion Proteins, Reporter, Restriction Mapping, Transcription},
pubstate = {published},
tppubtype = {article}
}
Gross I, Georgel Philippe, Kappler Christine, Reichhart Jean-Marc, Hoffmann Jules A
Drosophila immunity: a comparative analysis of the Rel proteins dorsal and Dif in the induction of the genes encoding diptericin and cecropin Journal Article
In: Nucleic Acids Res., vol. 24, no. 7, pp. 1238–1245, 1996, ISSN: 0305-1048.
Abstract | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, Base Sequence, DNA Primers, DNA-Binding Proteins, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, NF-kappa B, Nuclear Proteins, Peptides, Phosphoproteins, reichhart, Transcription, Transcription Factors, Transcriptional Activation
@article{gross_drosophila_1996,
title = {Drosophila immunity: a comparative analysis of the Rel proteins dorsal and Dif in the induction of the genes encoding diptericin and cecropin},
author = {I Gross and Philippe Georgel and Christine Kappler and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0305-1048},
year = {1996},
date = {1996-04-01},
journal = {Nucleic Acids Res.},
volume = {24},
number = {7},
pages = {1238--1245},
abstract = {In Drosophila, bacterial challenge induces the rapid transcription of several genes encoding potent antibacterial peptides. The upstream sequences of the diptericin and cecropin Al genes, which have been investigated in detail, contain two, respectively one sequence element homologous to the binding site of the mammalian nuclear factor kappaB. These elements have been shown to be mandatory for immune-induced transcription of both genes. Functional studies have shown that these kappaB-related elements can be the target for the Drosophila Rel proteins dorsal and Dif. Here we present a comparative analysis of the transactivating capacities of these proteins on reporter genes fused to either the diptericin or the cecropin kappaB-related motifs. We conclude from our results: (i) the kappaB motifs of the diptericin and cecropin genes are not functionally equivalent; (ii) the dorsal and Dif proteins have distinct DNA-binding characteristics; (iii) dorsal and Dif can heterodimerize in vitro; (iv) mutants containing no copies of dorsal and a single copy of Dif retain their full capacity to express the diptericin and cecropin genes in response to challenge.},
keywords = {Animals, Antimicrobial Cationic Peptides, Base Sequence, DNA Primers, DNA-Binding Proteins, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, NF-kappa B, Nuclear Proteins, Peptides, Phosphoproteins, reichhart, Transcription, Transcription Factors, Transcriptional Activation},
pubstate = {published},
tppubtype = {article}
}
Fehlbaum P, Bulet Philippe, Chernysh S, Briand J P, Roussel J P, Letellier L, Hetru Charles, Hoffmann Jules A
Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides Journal Article
In: Proc. Natl. Acad. Sci. U.S.A., vol. 93, no. 3, pp. 1221–1225, 1996, ISSN: 0027-8424.
Abstract | BibTeX | Tags: Amino Acid, Amphibian Proteins, Animals, Anti-Bacterial Agents, Anti-Infective Agents, Antimicrobial Cationic Peptides, Cyclic, Fungi, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemiptera, hoffmann, M3i, Mass Spectrometry, Microbial Sensitivity Tests, Peptides, Ranidae, Sequence Homology, Skin, Structure-Activity Relationship
@article{fehlbaum_structure-activity_1996,
title = {Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides},
author = {P Fehlbaum and Philippe Bulet and S Chernysh and J P Briand and J P Roussel and L Letellier and Charles Hetru and Jules A Hoffmann},
issn = {0027-8424},
year = {1996},
date = {1996-02-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {93},
number = {3},
pages = {1221--1225},
abstract = {Immune challenge to the insect Podisus maculiventris induces synthesis of a 21-residue peptide with sequence homology to frog skin antimicrobial peptides of the brevinin family. The insect and frog peptides have in common a C-terminally located disulfide bridge delineating a cationic loop. The peptide is bactericidal and fungicidal, exhibiting the largest antimicrobial spectrum observed so far for an insect defense peptide. An all-D-enantiomer is nearly inactive against Gram-negative bacteria and some Gram-positive strains but is fully active against fungi and other Gram-positive bacteria, suggesting that more than one mechanism accounts for the antimicrobial activity of this peptide. Studies with truncated synthetic isoforms underline the role of the C-terminal loop and flanking residues for the activity of this molecule for which we propose the name thanatin.},
keywords = {Amino Acid, Amphibian Proteins, Animals, Anti-Bacterial Agents, Anti-Infective Agents, Antimicrobial Cationic Peptides, Cyclic, Fungi, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemiptera, hoffmann, M3i, Mass Spectrometry, Microbial Sensitivity Tests, Peptides, Ranidae, Sequence Homology, Skin, Structure-Activity Relationship},
pubstate = {published},
tppubtype = {article}
}
Lemaitre Bruno, Kromer-Metzger E, Michaut Lydia, Nicolas E, Meister Marie, Georgel Philippe, Reichhart Jean-Marc, Hoffmann Jules A
A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense Journal Article
In: Proc. Natl. Acad. Sci. U.S.A., vol. 92, no. 21, pp. 9465–9469, 1995, ISSN: 0027-8424.
Abstract | BibTeX | Tags: Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Bacterial Infections, Base Sequence, Gene Expression Regulation, Genes, Glycopeptides, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, Male, Mutation, Mycoses, Nucleic Acid, Peptides, Protein Binding, Recessive, Regulatory Sequences, reichhart, Reporter, Survival Analysis
@article{lemaitre_recessive_1995,
title = {A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense},
author = {Bruno Lemaitre and E Kromer-Metzger and Lydia Michaut and E Nicolas and Marie Meister and Philippe Georgel and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0027-8424},
year = {1995},
date = {1995-10-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {92},
number = {21},
pages = {9465--9469},
abstract = {In this paper we report a recessive mutation, immune deficiency (imd), that impairs the inducibility of all genes encoding antibacterial peptides during the immune response of Drosophila. When challenged with bacteria, flies carrying this mutation show a lower survival rate than wild-type flies. We also report that, in contrast to the antibacterial peptides, the antifungal peptide drosomycin remains inducible in a homozygous imd mutant background. These results point to the existence of two different pathways leading to the expression of two types of target genes, encoding either the antibacterial peptides or the antifungal peptide drosomycin.},
keywords = {Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Bacterial Infections, Base Sequence, Gene Expression Regulation, Genes, Glycopeptides, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, Male, Mutation, Mycoses, Nucleic Acid, Peptides, Protein Binding, Recessive, Regulatory Sequences, reichhart, Reporter, Survival Analysis},
pubstate = {published},
tppubtype = {article}
}
Levashina Elena A, Ohresser S, Bulet Philippe, Reichhart Jean-Marc, Hetru Charles, Hoffmann Jules A
Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties Journal Article
In: Eur. J. Biochem., vol. 233, no. 2, pp. 694–700, 1995, ISSN: 0014-2956.
Abstract | BibTeX | Tags: Animals, Anti-Bacterial Agents, Antifungal Agents, Antimicrobial Cationic Peptides, bacteria, Base Sequence, Cells, Chromosome Mapping, Cloning, Cultured, Genetic, hoffmann, M3i, Molecular, Peptides, Proline, reichhart, Transcription
@article{levashina_metchnikowin_1995,
title = {Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties},
author = {Elena A Levashina and S Ohresser and Philippe Bulet and Jean-Marc Reichhart and Charles Hetru and Jules A Hoffmann},
issn = {0014-2956},
year = {1995},
date = {1995-10-01},
journal = {Eur. J. Biochem.},
volume = {233},
number = {2},
pages = {694--700},
abstract = {One of the characteristics of the host defense of higher insects is the rapid and transient synthesis of a variety of potent antimicrobial peptides. To date, several distinct inducible antimicrobial peptides or peptide families have been totally or partially characterized. We present here the isolation and characterization of a novel 26-residue proline-rich immune-inducible peptide from Drosophila, which exhibits both antibacterial (Gram-positive) and antifungal activities. Peptide sequencing and cDNA cloning indicate the presense of two isoforms in our Drosophila Oregon strain, which differ by one residue (His compared to Arg) as a consequence of a single nucleotide change. The gene, which maps in position 52A1-2 on the right arm of the second chromosome, is expressed in the fat body after immune challenge. The novel peptide, which we propose to name metchnikowin, is a member of a family of proline-rich peptides, and we discuss the possible evolutionary relationships within this family.},
keywords = {Animals, Anti-Bacterial Agents, Antifungal Agents, Antimicrobial Cationic Peptides, bacteria, Base Sequence, Cells, Chromosome Mapping, Cloning, Cultured, Genetic, hoffmann, M3i, Molecular, Peptides, Proline, reichhart, Transcription},
pubstate = {published},
tppubtype = {article}
}
Lemaitre Bruno, Meister Marie, Govind S, Georgel Philippe, Steward R, Reichhart Jean-Marc, Hoffmann Jules A
Functional analysis and regulation of nuclear import of dorsal during the immune response in Drosophila Journal Article
In: EMBO J., vol. 14, no. 3, pp. 536–545, 1995, ISSN: 0261-4189.
Abstract | BibTeX | Tags: Animals, Anti-Bacterial Agents, Anti-Infective Agents, Antimicrobial Cationic Peptides, Biological Transport, Cell Nucleus, Cell Surface, DNA-Binding Proteins, Fat Body, Gene Expression Regulation, Genetic, hoffmann, Immunity, Immunohistochemistry, Insect Hormones, Insect Proteins, M3i, Melanins, Membrane Glycoproteins, Mutation, Neoplasms, Nuclear Proteins, Phosphoproteins, Receptors, reichhart, Signal Transduction, Toll-Like Receptors, Transcription, Transcription Factors
@article{lemaitre_functional_1995,
title = {Functional analysis and regulation of nuclear import of dorsal during the immune response in Drosophila},
author = {Bruno Lemaitre and Marie Meister and S Govind and Philippe Georgel and R Steward and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0261-4189},
year = {1995},
date = {1995-01-01},
journal = {EMBO J.},
volume = {14},
number = {3},
pages = {536--545},
abstract = {In addition to its function in embryonic development, the NF-kappa B/rel-related gene dorsal (dl) of Drosophila is expressed in larval and adult fat body where its RNA expression is enhanced upon injury. Injury also leads to a rapid nuclear translocation of dl from the cytoplasm in fat body cells. Here we present data which strongly suggest that the nuclear localization of dl during the immune response is controlled by the Toll signaling pathway, comprising gene products that participate in the intracellular part of the embryonic dorsoventral pathway. We also report that in mutants such as Toll or cactus, which exhibit melanotic tumor phenotypes, dl is constitutively nuclear. Together, these results point to a potential link between the Toll signaling pathway and melanotic tumor induction. Although dl has been shown previously to bind to kappa B-related motifs within the promoter of the antibacterial peptide coding gene diptericin, we find that injury-induced expression of diptericin can occur in the absence of dl. Furthermore, the melanotic tumor phenotype of Toll and cactus is not dl dependent. These data underline the complexity of the Drosophila immune response. Finally, we observed that like other rel proteins, dl can control the level of its own transcription.},
keywords = {Animals, Anti-Bacterial Agents, Anti-Infective Agents, Antimicrobial Cationic Peptides, Biological Transport, Cell Nucleus, Cell Surface, DNA-Binding Proteins, Fat Body, Gene Expression Regulation, Genetic, hoffmann, Immunity, Immunohistochemistry, Insect Hormones, Insect Proteins, M3i, Melanins, Membrane Glycoproteins, Mutation, Neoplasms, Nuclear Proteins, Phosphoproteins, Receptors, reichhart, Signal Transduction, Toll-Like Receptors, Transcription, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
Cociancich S, Dupont A, Hegy G, Lanot R, Holder F, Hetru Charles, Hoffmann Jules A, Bulet Philippe
Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus Journal Article
In: Biochem. J., vol. 300 ( Pt 2), pp. 567–575, 1994, ISSN: 0264-6021.
Abstract | BibTeX | Tags: Amino Acid, Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Blood Proteins, Chromatography, Defensins, Gas Chromatography-Mass Spectrometry, Gel, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemiptera, Hemolymph, hoffmann, Insect Proteins, M3i, Peptides, Sequence Homology
@article{cociancich_novel_1994,
title = {Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus},
author = {S Cociancich and A Dupont and G Hegy and R Lanot and F Holder and Charles Hetru and Jules A Hoffmann and Philippe Bulet},
issn = {0264-6021},
year = {1994},
date = {1994-06-01},
journal = {Biochem. J.},
volume = {300 ( Pt 2)},
pages = {567--575},
abstract = {Insects belonging to the recent orders of the endopterygote clade (Lepidoptera, Diptera, Hymenoptera and Coleoptera) respond to bacterial challenge by the rapid and transient synthesis of a battery of potent antibacterial peptides which are secreted into their haemolymph. Here we present the first report on inducible antibacterial molecules in the sap-sucking bug Pyrrhocoris apterus, a representative species of the Hemiptera, which predated the Endoptergotes by at least 50 million years in evolution. We have isolated and characterized from immune blood of this species three novel peptides or polypeptides: (i) a 43-residue cysteine-rich anti-(Gram-positive bacteria) peptide which is a new member of the family of insect defensins; (ii) a 20-residue proline-rich peptide carrying an O-glycosylated substitution (N-acetylgalactosamine), active against Gram-negative bacteria; (iii) a 133-residue glycine-rich polypeptide also active against Gram-negative bacteria. The proline-rich peptide shows high sequence similarities with drosocin, an O-glycosylated antibacterial peptide from Drosophila, and also with the N-terminal domain of diptericin, an inducible 9 kDa antibacterial peptide from members of the order Diptera, whereas the glycine-rich peptide has similarities with the glycine-rich domain of diptericin. We discuss the evolutionary aspects of these findings.},
keywords = {Amino Acid, Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Blood Proteins, Chromatography, Defensins, Gas Chromatography-Mass Spectrometry, Gel, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemiptera, Hemolymph, hoffmann, Insect Proteins, M3i, Peptides, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Bulet Philippe, Cociancich S, Reuland M, Sauber F, Bischoff R, Hegy G, Dorsselaer Van A, Hetru Charles, Hoffmann Jules A
A novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata) Journal Article
In: Eur. J. Biochem., vol. 209, no. 3, pp. 977–984, 1992, ISSN: 0014-2956.
Abstract | BibTeX | Tags: Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Blood Bactericidal Activity, Blood Proteins, Defensins, Hemolymph, hoffmann, Insect Proteins, insects, Larva, M3i, Mass Spectrometry, Peptides
@article{bulet_novel_1992,
title = {A novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata)},
author = {Philippe Bulet and S Cociancich and M Reuland and F Sauber and R Bischoff and G Hegy and Van A Dorsselaer and Charles Hetru and Jules A Hoffmann},
issn = {0014-2956},
year = {1992},
date = {1992-11-01},
journal = {Eur. J. Biochem.},
volume = {209},
number = {3},
pages = {977--984},
abstract = {The injection of low doses of bacteria into the aquatic larvae of dragonflies (Aeschna cyanea, Odonata, Paleoptera) induces the appearance in their hemolymph of a potent antibacterial activity. We have isolated a 38-residue peptide from this hemolymph which is strongly active against Gram-positive bacteria and also shows activity against one of the Gram-negative bacteria which was tested. The peptide is a novel member of the insect defensin family of inducible antibacterial peptides, which had so far only been reported from the higher insect orders believed to have evolved 100 million years after the Paleoptera. Aeschna defensin is more potent than defensin from the dipteran Phormia, from which its structure differs in several interesting aspects, which are discussed in the paper.},
keywords = {Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Blood Bactericidal Activity, Blood Proteins, Defensins, Hemolymph, hoffmann, Insect Proteins, insects, Larva, M3i, Mass Spectrometry, Peptides},
pubstate = {published},
tppubtype = {article}
}
Hoffmann Jules A, Hoffmann Danièle
The inducible antibacterial peptides of dipteran insects Journal Article
In: Res. Immunol., vol. 141, no. 9, pp. 910–918, 1990, ISSN: 0923-2494.
BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, Defensins, Diptera, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Nucleic Acid, Proteins, Sequence Homology, Transcription
@article{hoffmann_inducible_1990,
title = {The inducible antibacterial peptides of dipteran insects},
author = {Jules A Hoffmann and Danièle Hoffmann},
issn = {0923-2494},
year = {1990},
date = {1990-12-01},
journal = {Res. Immunol.},
volume = {141},
number = {9},
pages = {910--918},
keywords = {Animals, Antimicrobial Cationic Peptides, Defensins, Diptera, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Nucleic Acid, Proteins, Sequence Homology, Transcription},
pubstate = {published},
tppubtype = {article}
}