Publications
2005
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}
}
2001
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}
}
2000
Imler Jean-Luc, Tauszig Servane, Jouanguy Emmanuelle, Forestier C, Hoffmann Jules A
LPS-induced immune response in Drosophila Journal Article
In: Journal of Endotoxin Research, vol. 6, no. 6, pp. 459–462, 2000, ISSN: 0968-0519.
Abstract | BibTeX | Tags: Animals, Biological, Cell Line, Cell Surface, Defensins, Genes, Genetic, hoffmann, imler, Insect, Insect Proteins, Lipopolysaccharides, M3i, Membrane Glycoproteins, Models, Mutation, Promoter Regions, Receptors, Signal Transduction, Toll-Like Receptors
@article{imler_lps-induced_2000,
title = {LPS-induced immune response in Drosophila},
author = {Jean-Luc Imler and Servane Tauszig and Emmanuelle Jouanguy and C Forestier and Jules A Hoffmann},
issn = {0968-0519},
year = {2000},
date = {2000-01-01},
journal = {Journal of Endotoxin Research},
volume = {6},
number = {6},
pages = {459--462},
abstract = {The study of the regulation of the inducible synthesis of antimicrobial peptides in Drosophila melanogaster has established this insect as a powerful model in which to study innate immunity. In particular, the molecular characterization of the regulatory pathway controlling the antifungal peptide drosomycin has revealed the importance of Toll receptors in innate immunity. We report here that injection of LPS into flies induces an immune response, suggesting that LPS receptors are used in Drosophila to detect Gram-negative bacteria infection. We have identified in the recently sequenced genome of Drosophila eight genes coding for Toll-like receptors in addition to Toll, which may function as LPS receptors. However, overexpression of a selection of these genes in tissue-culture cells does not result in up-regulation of the antibacterial peptide genes. These results are discussed in light of the recent data from genetic screens aimed at identifying the genes controlling the antibacterial response in Drosophila.},
keywords = {Animals, Biological, Cell Line, Cell Surface, Defensins, Genes, Genetic, hoffmann, imler, Insect, Insect Proteins, Lipopolysaccharides, M3i, Membrane Glycoproteins, Models, Mutation, Promoter Regions, Receptors, Signal Transduction, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
1999
Lamberty M, Ades S, Uttenweiler-Joseph S, Brookhart G, Bushey D, Hoffmann Jules A, Bulet Philippe
Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity Journal Article
In: J. Biol. Chem., vol. 274, no. 14, pp. 9320–9326, 1999, ISSN: 0021-9258.
Abstract | BibTeX | Tags: Amino Acid, Animals, Antifungal Agents, Capillary, Chromatography, Defensins, Electrophoresis, Escherichia coli, Hemolymph, High Pressure Liquid, hoffmann, Insect Proteins, Larva, Lepidoptera, M3i, Micrococcus luteus, Proteins, Sequence Homology
@article{lamberty_insect_1999,
title = {Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity},
author = {M Lamberty and S Ades and S Uttenweiler-Joseph and G Brookhart and D Bushey and Jules A Hoffmann and Philippe Bulet},
issn = {0021-9258},
year = {1999},
date = {1999-04-01},
journal = {J. Biol. Chem.},
volume = {274},
number = {14},
pages = {9320--9326},
abstract = {Lepidoptera have been reported to produce several antibacterial peptides in response to septic injury. However, in marked contrast to other insect groups, no inducible antifungal molecules had been described so far in this insect order. Surprisingly, also cysteine-rich antimicrobial peptides, which predominate in the antimicrobial defense of other insects, had not been discovered in Lepidoptera. Here we report the isolation from the hemolymph of immune induced larvae of the lepidopteran Heliothis virescens of a cysteine-rich molecule with exclusive antifungal activity. We have fully characterized this antifungal molecule, which has significant homology with the insect defensins, a large family of antibacterial peptides directed against Gram-positive strains. Interestingly, the novel peptide shows also similarities with the antifungal peptide drosomycin from Drosophila. Thus, Lepidoptera appear to have built their humoral immune response against bacteria on cecropins and attacins. In addition, we report that Lepidoptera have conferred antifungal properties to the well conserved structure of antibacterial insect defensins through amino acid replacements.},
keywords = {Amino Acid, Animals, Antifungal Agents, Capillary, Chromatography, Defensins, Electrophoresis, Escherichia coli, Hemolymph, High Pressure Liquid, hoffmann, Insect Proteins, Larva, Lepidoptera, M3i, Micrococcus luteus, Proteins, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Lowenberger C A, Smartt C T, Bulet Philippe, Ferdig M T, Severson D W, Hoffmann Jules A, Christensen B M
Insect immunity: molecular cloning, expression, and characterization of cDNAs and genomic DNA encoding three isoforms of insect defensin in Aedes aegypti Journal Article
In: Insect Mol. Biol., vol. 8, no. 1, pp. 107–118, 1999, ISSN: 0962-1075.
Abstract | BibTeX | Tags: Aedes, Amino Acid, Animals, Base Sequence, Blotting, Chromosome Mapping, Cloning, Complementary, Defensins, DNA, Gene Expression, Hemolymph, hoffmann, M3i, Molecular, Northern, Protein Isoforms, Proteins, Sequence Homology
@article{lowenberger_insect_1999,
title = {Insect immunity: molecular cloning, expression, and characterization of cDNAs and genomic DNA encoding three isoforms of insect defensin in Aedes aegypti},
author = {C A Lowenberger and C T Smartt and Philippe Bulet and M T Ferdig and D W Severson and Jules A Hoffmann and B M Christensen},
issn = {0962-1075},
year = {1999},
date = {1999-02-01},
journal = {Insect Mol. Biol.},
volume = {8},
number = {1},
pages = {107--118},
abstract = {Aedes aegypti were immune activated by injection with bacteria, and the expression of insect defensins was measured over time. Northern analyses indicated that defensin transcriptional activity continued for at least 21 days after bacterial injection, and up to 10 days after saline inoculation. Mature defensin levels in the haemolymph reached approximately 45 microM at 24 h post inoculation. cDNAs encoding the preprodefensins of three previously described mature Ae. aegypti defensins were amplified by PCR, cloned and sequenced. Genomic clones were amplified using primers designed against the cDNA sequence. Sequence comparison indicates that there is significant inter- and intra-isoform variability in the signal peptide and prodefensin sequences of defensin genes. Preprodefensin sequences of isoforms A and B are very similar, consisting of a signal peptide region of twenty amino acids, a prodefensin region of thirty-eight amino acids and a forty amino acid mature peptide domain. The sequence encoding isoform C is significantly different, comprising a signal peptide region of twenty-three amino acids, a prodefensin region of thirty-six amino acids, and the mature protein domain of forty amino acids. Analysis of the genomic clones of each isoform revealed one intron spatially conserved in the prodefensin region of all sequences. The intron in isoforms A and B is 64 nt long, and except for a 4 nt substitution in one clone, these intron sequences are identical. The intron in isoform C is 76 nt long and does not share significant identity with the intron sequences of isoforms A or B. The defensin gene mapped to chromosome 3, between two known loci, blt and LF168.},
keywords = {Aedes, Amino Acid, Animals, Base Sequence, Blotting, Chromosome Mapping, Cloning, Complementary, Defensins, DNA, Gene Expression, Hemolymph, hoffmann, M3i, Molecular, Northern, Protein Isoforms, Proteins, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Lowenberger C A, Kamal S, Chiles J, Paskewitz S, Bulet Philippe, Hoffmann Jules A, Christensen B M
Mosquito-Plasmodium interactions in response to immune activation of the vector Journal Article
In: Exp. Parasitol., vol. 91, no. 1, pp. 59–69, 1999, ISSN: 0014-4894.
Abstract | Links | BibTeX | Tags: Aedes, Animals, Anopheles, Culicidae, Defensins, Digestive System, Escherichia coli, Female, Genetic, Hemolymph, hoffmann, Insect Vectors, M3i, messenger, Micrococcus luteus, Plasmodium, Plasmodium berghei, Plasmodium gallinaceum, Proteins, Reverse Transcriptase Polymerase Chain Reaction, RNA, Transcription
@article{lowenberger_mosquito-plasmodium_1999,
title = {Mosquito-Plasmodium interactions in response to immune activation of the vector},
author = {C A Lowenberger and S Kamal and J Chiles and S Paskewitz and Philippe Bulet and Jules A Hoffmann and B M Christensen},
doi = {10.1006/expr.1999.4350},
issn = {0014-4894},
year = {1999},
date = {1999-01-01},
journal = {Exp. Parasitol.},
volume = {91},
number = {1},
pages = {59--69},
abstract = {During the development of Plasmodium sp. within the mosquito midgut, the parasite undergoes a series of developmental changes. The elongated ookinete migrates through the layers of the midgut where it forms the oocyst under the basal lamina. We demonstrate here that if Aedes aegypti or Anopheles gambiae, normally susceptible to Plasmodium gallinaceum and P. berghei, respectively, are immune activated by the injection of bacteria into the hemocoel, and subsequently are fed on an infectious bloodmeal, there is a significant reduction in the prevalence and mean intensity of infection of oocysts on the midgut. Only those mosquitoes immune activated prior to, or immediately after, parasite ingestion exhibit this reduction in parasite development. Mosquitoes immune activated 2-5 days after bloodfeeding show no differences in parasite burdens compared with naive controls. Northern analyses reveal that transcriptional activity for mosquito defensins is not detected in the whole bodies of Ae. aegypti from 4 h to 10 days after ingesting P. gallinaceum, suggesting that parasite ingestion, passage from the food bolus through the midgut, oocyst formation, and subsequent release of sporozoites into the hemolymph do not induce the production of defensin. However, reverse transcriptase-PCR of RNA isolated solely from the midguts of Ae. aegypti indicates that transcription of mosquito defensins occurs in the midguts of naive mosquitoes and those ingesting an infectious or noninfectious bloodmeal. Bacteria-challenged Ae. aegypti showed high levels of mature defensin in the hemolymph that correlate with a lower prevalence and mean intensity of infection with oocysts. Because few oocysts were found on the midgut of immune-activated mosquitoes, the data suggest that some factor, induced by bacterial challenge, kills the parasite at a preoocyst stage.},
keywords = {Aedes, Animals, Anopheles, Culicidae, Defensins, Digestive System, Escherichia coli, Female, Genetic, Hemolymph, hoffmann, Insect Vectors, M3i, messenger, Micrococcus luteus, Plasmodium, Plasmodium berghei, Plasmodium gallinaceum, Proteins, Reverse Transcriptase Polymerase Chain Reaction, RNA, Transcription},
pubstate = {published},
tppubtype = {article}
}
1998
Shahabuddin M, Fields I, Bulet Philippe, Hoffmann Jules A, Miller L H
Plasmodium gallinaceum: differential killing of some mosquito stages of the parasite by insect defensin Journal Article
In: Exp. Parasitol., vol. 89, no. 1, pp. 103–112, 1998, ISSN: 0014-4894.
Abstract | Links | BibTeX | Tags: Aedes, Animals, Anti-Infective Agents, Blood Proteins, Defensins, Diptera, hoffmann, Insect Vectors, insects, M3i, Plasmodium gallinaceum, Zygote
@article{shahabuddin_plasmodium_1998,
title = {Plasmodium gallinaceum: differential killing of some mosquito stages of the parasite by insect defensin},
author = {M Shahabuddin and I Fields and Philippe Bulet and Jules A Hoffmann and L H Miller},
doi = {10.1006/expr.1998.4212},
issn = {0014-4894},
year = {1998},
date = {1998-05-01},
journal = {Exp. Parasitol.},
volume = {89},
number = {1},
pages = {103--112},
abstract = {We examined several insect antimicrobial peptides to study their effect on Plasmodium gallinaceum zygotes, ookinetes, oocysts, and sporozoites. Only two insect defensins-Aeschna cyanea (dragon fly) and Phormia terranovae (flesh fly)-had a profound toxic effect on the oocysts in Aedes aegypti and on isolated sporozoites. The defensins affected the oocysts in a time-dependent manner. Injecting the peptide into the hemolymph 1 or 2 days after an infectious blood meal had no significant effect on prevalence of infection or relative oocyst density per mosquito. When injected 3 days after parasite ingestion, the relative oocyst density was significantly reduced. Injection on day 4 or later damaged the developing oocysts, although the oocysts density per mosquito was not significantly different when examined on day 8. The oocysts were swollen or had extensive internal vacuolization. The peptides had no detectable effect on the early stages of the parasite: the zygotes and ookinetes tested in vitro. Both the defensins were highly toxic to isolated sporozoites in vitro as indicated by disruption of the membrane permeability barrier, a change in morphology, and loss of motility. In contrast to the toxicity of cecropin and magainin for mosquitoes, defensin, at concentrations that kill parasites, is not toxic to mosquitoes, suggesting that defensin should be studied further as a potential molecule to block sporogonic development of Plasmodium.},
keywords = {Aedes, Animals, Anti-Infective Agents, Blood Proteins, Defensins, Diptera, hoffmann, Insect Vectors, insects, M3i, Plasmodium gallinaceum, Zygote},
pubstate = {published},
tppubtype = {article}
}
1997
Hoffmann Jules A
Immune responsiveness in vector insects Journal Article
In: Proc. Natl. Acad. Sci. U.S.A., vol. 94, no. 21, pp. 11152–11153, 1997, ISSN: 0027-8424.
BibTeX | Tags: Animals, Anopheles, bacteria, Blood Proteins, Defensins, hoffmann, Humans, Insect Vectors, Life Cycle Stages, M3i, Malaria, Mammals, Plasmodium
@article{hoffmann_immune_1997,
title = {Immune responsiveness in vector insects},
author = {Jules A Hoffmann},
issn = {0027-8424},
year = {1997},
date = {1997-10-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {94},
number = {21},
pages = {11152--11153},
keywords = {Animals, Anopheles, bacteria, Blood Proteins, Defensins, hoffmann, Humans, Insect Vectors, Life Cycle Stages, M3i, Malaria, Mammals, Plasmodium},
pubstate = {published},
tppubtype = {article}
}
1996
Charlet Maurice, Chernysh S, Philippe H, Hetru Charles, Hoffmann Jules A, Bulet Philippe
Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis Journal Article
In: J. Biol. Chem., vol. 271, no. 36, pp. 21808–21813, 1996, ISSN: 0021-9258.
Abstract | BibTeX | Tags: Amino Acid, Animals, Anti-Infective Agents, Antifungal Agents, Bivalvia, Blood Proteins, Chromatography, Cysteine, Defensins, High Pressure Liquid, hoffmann, M3i, Molecular Weight, Phylogeny, Sequence Homology
@article{charlet_innate_1996,
title = {Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis},
author = {Maurice Charlet and S Chernysh and H Philippe and Charles Hetru and Jules A Hoffmann and Philippe Bulet},
issn = {0021-9258},
year = {1996},
date = {1996-09-01},
journal = {J. Biol. Chem.},
volume = {271},
number = {36},
pages = {21808--21813},
abstract = {We have isolated from the blood of immune-challenged and untreated mussels (Mytilus edulis) antibacterial and antifungal peptides. We have characterized two isoforms of a novel 34-residue, cysteine-rich, peptide with potent bactericidal activity and partially characterized a novel 6.2-kDa antifungal peptide containing 12 cysteines. We report the presence of two members of the insect defensin family of antibacterial peptides and provide a phylogenetic analysis that indicates that mollusc and arthropod defensins have a common ancestry. Our data argue that circulating antimicrobial peptides represent an ancient host defense mechanism that predated the separation between molluscs and arthropods at the root of the Cambrian, about 545 million years ago.},
keywords = {Amino Acid, Animals, Anti-Infective Agents, Antifungal Agents, Bivalvia, Blood Proteins, Chromatography, Cysteine, Defensins, High Pressure Liquid, hoffmann, M3i, Molecular Weight, Phylogeny, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Richman A M, Bulet Philippe, Hetru Charles, Barillas-Mury Carolina, Hoffmann Jules A, Kafalos Fotis C
Inducible immune factors of the vector mosquito Anopheles gambiae: biochemical purification of a defensin antibacterial peptide and molecular cloning of preprodefensin cDNA Journal Article
In: Insect Mol. Biol., vol. 5, no. 3, pp. 203–210, 1996, ISSN: 0962-1075.
Abstract | BibTeX | Tags: Amino Acid, Animals, Anopheles, Base Sequence, Blood Bactericidal Activity, Blood Proteins, Cloning, Complementary, Defensins, DNA, Escherichia coli, Female, Gene Expression, Genes, hoffmann, Insect, Insect Vectors, Larva, M3i, Micrococcus luteus, Molecular, Sequence Homology
@article{richman_inducible_1996,
title = {Inducible immune factors of the vector mosquito Anopheles gambiae: biochemical purification of a defensin antibacterial peptide and molecular cloning of preprodefensin cDNA},
author = {A M Richman and Philippe Bulet and Charles Hetru and Carolina Barillas-Mury and Jules A Hoffmann and Fotis C Kafalos},
issn = {0962-1075},
year = {1996},
date = {1996-08-01},
journal = {Insect Mol. Biol.},
volume = {5},
number = {3},
pages = {203--210},
abstract = {Larvae of the mosquito vector of human malaria, Anopheles gambiae, were inoculated with bacteria and extracts were biochemically fractionated by reverse-phase HPLC. Multiple induced polypeptides and antibacterial activities were observed following bacterial infection, including a member of the insect defensin family of antibacterial proteins. A cDNA encoding An. gambiae preprodefensin was isolated using PCR primers based on phylogenetically conserved sequences. The mature peptide is highly conserved, but the signal and propeptide segments are not, relative to corresponding defensin sequences of other insects. Defensin expression is induced in response to bacterial infection, in both adult and larval stages. In contrast, pupae express defensin mRNA constitutively. Defensin expression may prove a valuable molecular marker to monitor the An. gambiae host response to infection by parasitic protozoa of medical importance.},
keywords = {Amino Acid, Animals, Anopheles, Base Sequence, Blood Bactericidal Activity, Blood Proteins, Cloning, Complementary, Defensins, DNA, Escherichia coli, Female, Gene Expression, Genes, hoffmann, Insect, Insect Vectors, Larva, M3i, Micrococcus luteus, Molecular, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Lowenberger C A, Ferdig M T, Bulet Philippe, Khalili S, Hoffmann Jules A, Christensen B M
Aedes aegypti: induced antibacterial proteins reduce the establishment and development of Brugia malayi Journal Article
In: Exp. Parasitol., vol. 83, no. 2, pp. 191–201, 1996, ISSN: 0014-4894.
Abstract | Links | BibTeX | Tags: Aedes, Analysis of Variance, Animals, Anti-Bacterial Agents, Base Sequence, Blood Proteins, Blotting, Brugia malayi, Culicidae, Defensins, DNA, Escherichia coli, Fat Body, Genetic, Gerbillinae, hoffmann, M3i, Micrococcus luteus, Microfilaria, Northern, RNA, Transcription
@article{lowenberger_aedes_1996,
title = {Aedes aegypti: induced antibacterial proteins reduce the establishment and development of Brugia malayi},
author = {C A Lowenberger and M T Ferdig and Philippe Bulet and S Khalili and Jules A Hoffmann and B M Christensen},
doi = {10.1006/expr.1996.0066},
issn = {0014-4894},
year = {1996},
date = {1996-07-01},
journal = {Exp. Parasitol.},
volume = {83},
number = {2},
pages = {191--201},
abstract = {The effect of host immune activation on the development of Brugia malayi in one susceptible and four refractory strains of Aedes aegypti and in Armigeres subalbatus was assessed. A. aegypti that were immune activated by the injection of saline or bacteria 24 hr before feeding on a B. malayi-infected gerbil had significantly reduced prevalences and mean intensities of infection from those of naive controls when exposed to bloodmeals with low (105 mf/20 microliters) and medium (160 mf/20 microliters) microfilaremias. At a higher microfilaremia (237 mf/20 microliters) there were no significant differences in mean intensities, suggesting that the number of parasites ingested may affect the host's ability to mount an effective defense response. Because the major immune proteins in A. aegypti are defensins, we did Northern analyses of fat body RNA 8 hr after immune activation or bloodfeeding. All mosquitoes demonstrated rapid transcriptional activity for defensins following immune activation by intrathoracic inoculation with either saline or bacteria. However, no strain of A. aegypti, susceptible or refractory to B. malayi, nor Ar. subalbatus produced defensin transcripts after bloodfeeding on an uninfected or a B. malayi-infected gerbil. These data suggest that inducible immune proteins of mosquitoes can reduce the prevalence and mean intensity of infections with ingested parasites, but these proteins are not expressed routinely after parasite ingestion and midgut penetration and probably do not contribute to existing refractory mechanisms. Immune proteins such as defensins, however, represent potential candidates to genetically engineer mosquitoes for resistance to filarial worms.},
keywords = {Aedes, Analysis of Variance, Animals, Anti-Bacterial Agents, Base Sequence, Blood Proteins, Blotting, Brugia malayi, Culicidae, Defensins, DNA, Escherichia coli, Fat Body, Genetic, Gerbillinae, hoffmann, M3i, Micrococcus luteus, Microfilaria, Northern, RNA, Transcription},
pubstate = {published},
tppubtype = {article}
}
1995
Lowenberger C, Bulet Philippe, Charlet Maurice, Hetru Charles, Hodgeman B, Christensen B M, Hoffmann Jules A
Insect immunity: isolation of three novel inducible antibacterial defensins from the vector mosquito, Aedes aegypti Journal Article
In: Insect Biochem. Mol. Biol., vol. 25, no. 7, pp. 867–873, 1995, ISSN: 0965-1748.
Abstract | BibTeX | Tags: Aedes, Amino Acid, Animals, Anti-Bacterial Agents, Blood Proteins, Defensins, Escherichia coli, Gram-Negative Bacteria, Gram-Positive Bacteria, hoffmann, Immunity, Insect Vectors, M3i, Micrococcus luteus, Sequence Homology, Stereoisomerism
@article{lowenberger_insect_1995,
title = {Insect immunity: isolation of three novel inducible antibacterial defensins from the vector mosquito, Aedes aegypti},
author = {C Lowenberger and Philippe Bulet and Maurice Charlet and Charles Hetru and B Hodgeman and B M Christensen and Jules A Hoffmann},
issn = {0965-1748},
year = {1995},
date = {1995-07-01},
journal = {Insect Biochem. Mol. Biol.},
volume = {25},
number = {7},
pages = {867--873},
abstract = {The injection of Escherichia coli and Micrococcus luteus into the hemocoel of Aedes aegypti induces a potent antibacterial activity in the hemolymph. We have purified and fully characterized three 40-residue antibacterial peptides from the hemolymph of bacteria-challenged mosquitoes that are absent in naive mosquitoes. The peptides are potently active against Gram-positive bacteria and against one of the Gram-negative bacteria that were tested. The amino acid sequences clearly show that the three peptides are novel isoforms of the insect defensin family of antibacterial peptides. They differ from each other by one or two amino acid residues. We present here the complete amino acid sequences of the three isoforms and the activity spectrum of the predominant Aedes defensin.},
keywords = {Aedes, Amino Acid, Animals, Anti-Bacterial Agents, Blood Proteins, Defensins, Escherichia coli, Gram-Negative Bacteria, Gram-Positive Bacteria, hoffmann, Immunity, Insect Vectors, M3i, Micrococcus luteus, Sequence Homology, Stereoisomerism},
pubstate = {published},
tppubtype = {article}
}
Cornet B, Bonmatin J M, Hetru Charles, Hoffmann Jules A, Ptak M, Vovelle F
Refined three-dimensional solution structure of insect defensin A Journal Article
In: Structure, vol. 3, no. 5, pp. 435–448, 1995, ISSN: 0969-2126.
Abstract | BibTeX | Tags: Amino Acid, Animals, Bacteriolysis, Chemistry, Defensins, Diptera, Gram-Positive Bacteria, hoffmann, Hydrogen Bonding, Insect Hormones, M3i, Magnetic Resonance Spectroscopy, Models, Molecular, Physical, Physicochemical Phenomena, Protein Conformation, Recombinant Proteins, Sequence Homology, Solutions, Structure-Activity Relationship
@article{cornet_refined_1995,
title = {Refined three-dimensional solution structure of insect defensin A},
author = {B Cornet and J M Bonmatin and Charles Hetru and Jules A Hoffmann and M Ptak and F Vovelle},
issn = {0969-2126},
year = {1995},
date = {1995-05-01},
journal = {Structure},
volume = {3},
number = {5},
pages = {435--448},
abstract = {BACKGROUND: Insect defensin A is a basic 4 kDa protein secreted by Phormia terranovae larvae in response to bacterial challenges or injuries. Previous biological tests suggest that the bacterial cytoplasmic membrane is the target of defensin A. The structural study of this protein is the first step towards establishing a structure-activity relationship and forms the basis for understanding its antibiotic activity at the molecular level. RESULTS: We describe a refined model of the three-dimensional structure of defensin A derived from an extensive analysis of 786 inter-proton nuclear Overhauser effects. The backbone fold involves an N-terminal loop and an alpha-helical fragment followed by an antiparallel beta-structure. The helix and the beta-structure are connected by two of the three disulphide bridges present in defensin A, forming a so-called 'cysteine-stabilized alpha beta' (CS alpha beta) motif. The N-terminal loop, which is locally well defined, can occupy different positions with respect to the other moieties of the molecule. CONCLUSIONS: The CS alpha beta motif, which forms the core of the defensin A structure, appears to be a common organization for several families of small proteins with toxic properties. The distribution of amino acid side chains in the protein structure creates several hydrophobic or hydrophilic patches. This leads us to propose that the initial step in the action of positively charged defensin A molecules with cytoplasmic membranes may involve interactions with acidic phospholipids.},
keywords = {Amino Acid, Animals, Bacteriolysis, Chemistry, Defensins, Diptera, Gram-Positive Bacteria, hoffmann, Hydrogen Bonding, Insect Hormones, M3i, Magnetic Resonance Spectroscopy, Models, Molecular, Physical, Physicochemical Phenomena, Protein Conformation, Recombinant Proteins, Sequence Homology, Solutions, Structure-Activity Relationship},
pubstate = {published},
tppubtype = {article}
}
Hoffmann Jules A
Innate immunity of insects Journal Article
In: Curr. Opin. Immunol., vol. 7, no. 1, pp. 4–10, 1995, ISSN: 0952-7915.
Abstract | BibTeX | Tags: Animals, Anti-Bacterial Agents, Blood Proteins, Cellular, Defensins, Gene Expression Regulation, hoffmann, Immunity, Innate, insects, M3i, Peptides
@article{hoffmann_innate_1995,
title = {Innate immunity of insects},
author = {Jules A Hoffmann},
issn = {0952-7915},
year = {1995},
date = {1995-02-01},
journal = {Curr. Opin. Immunol.},
volume = {7},
number = {1},
pages = {4--10},
abstract = {Insects are particularly resistant to microorganisms. Their host-defense system relies on several innate reactions: upon injury, the immediate onset of two proteolytic cascades leading to localized blood clotting and to melanization, the latter process involving production of cytotoxic molecules (namely reactive oxygen intermediates); the phagocytosis of bacteria and the encapsulation of larger parasites by blood cells; the induced synthesis by the fat body of a battery of potent antimicrobial peptides/polypeptides which are secreted into the hemolymph where they act synergistically to kill the invading microorganisms. The insect host defence system shares many of the basic characteristics of the mammalian acute phase response, especially at the level of the coordinate control of gene expression, where similar cis-regulatory and inducible transactivators appear to play key functions. The powerful techniques developed to study the genetics of Drosophila provide a unique opportunity to dissect the development and differentiation of this primordial immune system and may contribute to our understanding of the innate immune response in higher organisms.},
keywords = {Animals, Anti-Bacterial Agents, Blood Proteins, Cellular, Defensins, Gene Expression Regulation, hoffmann, Immunity, Innate, insects, M3i, Peptides},
pubstate = {published},
tppubtype = {article}
}
1994
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}
}
Dimarcq Jean-Luc, Hoffmann Danièle, Meister Marie, Bulet Philippe, Lanot R, Reichhart Jean-Marc, Hoffmann Jules A
Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin. A study in insect immunity Journal Article
In: Eur. J. Biochem., vol. 221, no. 1, pp. 201–209, 1994, ISSN: 0014-2956.
Abstract | BibTeX | Tags: Animals, Base Sequence, Blood Proteins, Chromosome Mapping, Cloning, Complementary, Defensins, DNA, Gene Expression, Genetic, Gram-Positive Bacteria, hoffmann, Larva, M3i, Molecular, Molecular Structure, Nucleic Acid, Protein Precursors, Regulatory Sequences, reichhart, Transcription
@article{dimarcq_characterization_1994,
title = {Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin. A study in insect immunity},
author = {Jean-Luc Dimarcq and Danièle Hoffmann and Marie Meister and Philippe Bulet and R Lanot and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0014-2956},
year = {1994},
date = {1994-04-01},
journal = {Eur. J. Biochem.},
volume = {221},
number = {1},
pages = {201--209},
abstract = {Insect defensins are a family of 4-kDa, cationic, inducible antibacterial peptides which bear six cysteine residues engaged in three intramolecular disulfide bridges. They owe their name to certain sequence similarities with defensins from mammalian neutrophiles and macrophages. We report the characterization of a novel defensin isoform from Drosophila and the cloning of the gene encoding a preprodefensin. The gene, which is intronless and present in a single copy/haploid genome, maps at position 46CD on the right arm of the second chromosome. The analysis of the upstream region of the gene reveals the presence of multiple putative cis-regulatory sequences similar to mammalian regulatory motifs of acute-phase-response genes. Transcriptional profiles indicate that the Drosophila defensin gene is induced by bacterial challenge with acute-phase kinetics. It is also expressed in the absence of immune challenge during metamorphosis. These and other data on the Drosophila defensin gene lead us to suggest that insect and mammalian defensins have evolved independently.},
keywords = {Animals, Base Sequence, Blood Proteins, Chromosome Mapping, Cloning, Complementary, Defensins, DNA, Gene Expression, Genetic, Gram-Positive Bacteria, hoffmann, Larva, M3i, Molecular, Molecular Structure, Nucleic Acid, Protein Precursors, Regulatory Sequences, reichhart, Transcription},
pubstate = {published},
tppubtype = {article}
}
1992
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, Hetru Charles
Insect defensins: inducible antibacterial peptides Journal Article
In: Immunol. Today, vol. 13, no. 10, pp. 411–415, 1992, ISSN: 0167-5699.
Abstract | Links | BibTeX | Tags: Amino Acid, Animals, Bacterial Infections, Blood Bactericidal Activity, Blood Proteins, Defensins, hoffmann, insects, M3i, Peptides, Sequence Homology
@article{hoffmann_insect_1992,
title = {Insect defensins: inducible antibacterial peptides},
author = {Jules A Hoffmann and Charles Hetru},
doi = {10.1016/0167-5699(92)90092-L},
issn = {0167-5699},
year = {1992},
date = {1992-10-01},
journal = {Immunol. Today},
volume = {13},
number = {10},
pages = {411--415},
abstract = {In response to bacterial challenge or trauma, insects produce a battery of bactericidal or bacteriostatic molecules with a broad spectrum of activity against Gram-positive and/or Gram-negative bacteria; most are small-sized cationic peptides. This review focuses on insect defensins, a large group of inducible antibacterial peptides that are present both in ancient and recent insect orders. This immune response of insects shares many of the characteristics of the mammalian acute phase response.},
keywords = {Amino Acid, Animals, Bacterial Infections, Blood Bactericidal Activity, Blood Proteins, Defensins, hoffmann, insects, M3i, Peptides, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Bonmatin J M, Bonnat J L, Gallet X, Vovelle F, Ptak M, Reichhart Jean-Marc, Hoffmann Jules A, Keppi E, Legrain M, Achstetter T
Two-dimensional 1H NMR study of recombinant insect defensin A in water: resonance assignments, secondary structure and global folding Journal Article
In: J. Biomol. NMR, vol. 2, no. 3, pp. 235–256, 1992, ISSN: 0925-2738.
Abstract | BibTeX | Tags: Animals, Defensins, hoffmann, Hydrogen, Insect Hormones, insects, M3i, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Conformation, Recombinant Proteins, reichhart, Saccharomyces cerevisiae, Thermodynamics
@article{bonmatin_two-dimensional_1992,
title = {Two-dimensional 1H NMR study of recombinant insect defensin A in water: resonance assignments, secondary structure and global folding},
author = {J M Bonmatin and J L Bonnat and X Gallet and F Vovelle and M Ptak and Jean-Marc Reichhart and Jules A Hoffmann and E Keppi and M Legrain and T Achstetter},
issn = {0925-2738},
year = {1992},
date = {1992-01-01},
journal = {J. Biomol. NMR},
volume = {2},
number = {3},
pages = {235--256},
abstract = {A 500 MHz 2D 1H NMR study of recombinant insect defensin A is reported. This defense protein of 40 residues contains 3 disulfide bridges, is positively charged and exhibits antibacterial properties. 2D NMR maps of recombinant defensin A were fully assigned and secondary structure elements were localized. The set of NOE connectivities, 3JNH-alpha H coupling constants as well as 1H/2H exchange rates and delta delta/delta T temperature coefficients of NH protons strongly support the existence of an alpha-helix (residues 14-24) and of an antiparallel beta-sheet (residues 27-40). Models of the backbone folding were generated by using the DISMAN program and energy refined by using the AMBER program. This was done on the basis of: (i) 133 selected NOEs, (ii) 21 dihedral restraints from 3JNH-alpha H coupling constants, (iii) 12 hydrogen bonds mostly deduced from 1H/2H exchange rates or temperature coefficients, in addition to 9 initial disulfide bridge covalent constraints. The two secondary structure elements and the two bends connecting them involve approximately 70% of the total number of residues, which impose some stability in the C-terminal part of the molecule. The remaining N-terminal fragment forms a less well defined loop. This spatial organization, in which a beta-sheet is linked to an alpha-helix by two disulfide bridges and to a large loop by a third disulfide bridge, is rather similar to that found in scorpion charybdotoxin and seems to be partly present in several invertebrate toxins.},
keywords = {Animals, Defensins, hoffmann, Hydrogen, Insect Hormones, insects, M3i, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Conformation, Recombinant Proteins, reichhart, Saccharomyces cerevisiae, Thermodynamics},
pubstate = {published},
tppubtype = {article}
}
1991
Bulet Philippe, Cociancich S, Dimarcq Jean-Luc, Lambert J, Reichhart Jean-Marc, Hoffmann Danièle, Hetru Charles, Hoffmann Jules A
Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family Journal Article
In: J. Biol. Chem., vol. 266, no. 36, pp. 24520–24525, 1991, ISSN: 0021-9258.
Abstract | BibTeX | Tags: Animals, Antibody Formation, Beetles, Blood Bactericidal Activity, Blood Proteins, Chromatography, Defensins, Hemolymph, High Pressure Liquid, hoffmann, Insect Hormones, Insect Proteins, M3i, reichhart
@article{bulet_insect_1991,
title = {Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family},
author = {Philippe Bulet and S Cociancich and Jean-Luc Dimarcq and J Lambert and Jean-Marc Reichhart and Danièle Hoffmann and Charles Hetru and Jules A Hoffmann},
issn = {0021-9258},
year = {1991},
date = {1991-12-01},
journal = {J. Biol. Chem.},
volume = {266},
number = {36},
pages = {24520--24525},
abstract = {Injection of heat-killed bacteria into larvae of the large tenebrionid beetle Zophobas atratus (Insecta, Endopterygota, Coleoptera) results in the appearance in the hemolymph of a potent antibacterial activity as evidenced by a plate growth inhibition assay. We have isolated three peptides (A-C) from this immune hemolymph which probably account for most of this activity. Their primary structures were established by a combination of peptide sequencing and molecular mass determination by mass spectrometry. Peptide A, which is bactericidal against Gram-negative cells, is a 74-residue glycine-rich molecule with no sequence homology to known peptides. We propose the name coleoptericin for this novel inducible antibacterial peptide. Peptides B and C are isoforms of a 43-residue peptide which contains 6 cysteines and shows significant sequence homology to insect defensins, initially reported from dipteran insects. This peptide is active against Gram-positive bacteria. The results are discussed in connection with recent studies on inducible antibacterial peptides present in the three other major orders of the endopterygote clade of insects: the Lepidoptera, Diptera, and Hymenoptera.},
keywords = {Animals, Antibody Formation, Beetles, Blood Bactericidal Activity, Blood Proteins, Chromatography, Defensins, Hemolymph, High Pressure Liquid, hoffmann, Insect Hormones, Insect Proteins, M3i, reichhart},
pubstate = {published},
tppubtype = {article}
}
Lepage P, Bitsch F, Roecklin D, Keppi E, Dimarcq Jean-Luc, Reichhart Jean-Marc, Hoffmann Jules A, Roitsch C, Dorsselaer Van A
Determination of disulfide bridges in natural and recombinant insect defensin A Journal Article
In: Eur. J. Biochem., vol. 196, no. 3, pp. 735–742, 1991, ISSN: 0014-2956.
Abstract | BibTeX | Tags: Animals, Blood Proteins, Defensins, Diptera, Disulfides, Hemolymph, hoffmann, M3i, Mass Spectrometry, Recombinant Proteins, reichhart
@article{lepage_determination_1991,
title = {Determination of disulfide bridges in natural and recombinant insect defensin A},
author = {P Lepage and F Bitsch and D Roecklin and E Keppi and Jean-Luc Dimarcq and Jean-Marc Reichhart and Jules A Hoffmann and C Roitsch and Van A Dorsselaer},
issn = {0014-2956},
year = {1991},
date = {1991-01-01},
journal = {Eur. J. Biochem.},
volume = {196},
number = {3},
pages = {735--742},
abstract = {The primary-structure comparison of natural insect defensin A from Phormia terranovae and recombinant insect defensin A from Saccharomyces cerevisiae has been accomplished using a combination of Edman degradation and liquid secondary ion mass spectrometry. The natural and recombinant proteins have the same primary structure with identical disulfide-bond designations (formula; see text) as determined from the peptides obtained after thermolysin digestion. The combined use of Edman degradation and mass spectometry allowed the disulfide-bridge structure to be determined with a total of only 40 micrograms (9.9 nmol) natural peptide. Mass spectrometry provides a rapid means of disulfide-bridge verification, requiring not more than 20 micrograms recombinant insect defensin A, which is compatible with use in batch analysis.},
keywords = {Animals, Blood Proteins, Defensins, Diptera, Disulfides, Hemolymph, hoffmann, M3i, Mass Spectrometry, Recombinant Proteins, reichhart},
pubstate = {published},
tppubtype = {article}
}
1990
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}
}
Dimarcq Jean-Luc, Zachary Daniel, Hoffmann Jules A, Hoffmann Danièle, Reichhart Jean-Marc
Insect immunity: expression of the two major inducible antibacterial peptides, defensin and diptericin, in Phormia terranovae Journal Article
In: EMBO J., vol. 9, no. 8, pp. 2507–2515, 1990, ISSN: 0261-4189.
Abstract | BibTeX | Tags: Animals, Anti-Bacterial Agents, Base Sequence, Blood Proteins, Cloning, Defensins, Diptera, Gene Expression, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Molecular, Nucleic Acid Hybridization, Oligonucleotide Probes, Protein Conformation, reichhart
@article{dimarcq_insect_1990,
title = {Insect immunity: expression of the two major inducible antibacterial peptides, defensin and diptericin, in Phormia terranovae},
author = {Jean-Luc Dimarcq and Daniel Zachary and Jules A Hoffmann and Danièle Hoffmann and Jean-Marc Reichhart},
issn = {0261-4189},
year = {1990},
date = {1990-08-01},
journal = {EMBO J.},
volume = {9},
number = {8},
pages = {2507--2515},
abstract = {Injections of low doses of bacteria into larvae of Phormia terranovae induce the appearance of potent bactericidal peptides in the blood, among which predominate the anti-Gram positive insect defensins and the anti-Gram negative diptericins. Insect defensins show significant homologies to mammalian (including human) microbicidal peptides present in polymorphonuclear leukocytes and macrophages. We report the molecular cloning of cDNAs and primer extension studies which indicate that insect defensin is produced as a prepro-peptide yielding mature defensin A (40 residues) after cleavage of a putative signal peptide (23 residues) and a prosequence (34 residues). Previous studies have established that diptericin (82 residues) is matured from a pre-peptide by cleavage of a putative signal peptide (19 residues) and C-terminal amidation. Using oligonucleotide probes complementary to the sequences of the mRNAs for defensin and diptericin, we show by in situ hybridization that both antibacterial peptides are concomitantly synthesized by the same cells: thrombocytoids, a specialized blood cell type, and adipocytes. Transcriptional studies based on hybridization of RNAs to cDNAs of defensin and diptericin indicate that the transcription of both genes is induced regardless of the nature of the stimulus (injection of Gram positive or Gram negative bacteria, lipopolysaccharides). Even a sterile injury applied to axenically raised larvae is efficient in inducing the transcription of both genes suggesting that the local disruption of the integument aspecifically initiates a signalling mechanism which the thrombocytoids and the adipocytes are able to interpret. The transcription of immune genes is relatively short lived and a second challenge yields a response similar to that of the first stimulus, indicating that the experimental insects do not keep a 'memory' of their first injection.},
keywords = {Animals, Anti-Bacterial Agents, Base Sequence, Blood Proteins, Cloning, Defensins, Diptera, Gene Expression, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Molecular, Nucleic Acid Hybridization, Oligonucleotide Probes, Protein Conformation, reichhart},
pubstate = {published},
tppubtype = {article}
}