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M3i
Insect Models of Innate Immunity
Publications
1996
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}
}
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.
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}
}
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.
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}
}
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.
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}
}
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.