Imagerie

@article{Olmo_2019,

title = {The insect reservoir of biodiversity for viruses and for antiviral mechanisms},

author = {RP Olmo and NE Martins and ERGR Aguiar and JT Marques and JL Imler},

url = {https://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652019000600604&lng=en&nrm=iso&tlng=en},

doi = {10.1590/0001-3765201920190122},

year  = {2019},

date = {2019-06-03},

journal = { An Acad Bras Cienc },

volume = {91},

number = {Suppl 3},

pages = {e20190122},

abstract = {Insects are the most diverse group of animals. They can be infected by an extraordinary diversity of viruses. Among them, arthropod-borne viruses (arboviruses) can be transmitted to humans. High-throughput sequencing of small RNAs from insects provides insight into their virome, which may help understand the dynamics of vector borne infectious diseases. Furthermore, investigating the mechanisms that restrict viral infections in insects points to genetic innovations that may inspire novel antiviral strategies. },

keywords = {antiviral immunity, imler, insects, M3i, Marques, metagenomics, restriction factors, RNA Interference, virome},

pubstate = {published},

tppubtype = {article}

}

@article{aguiar_sequence-independent_2015,

title = {Sequence-independent characterization of viruses based on the pattern of viral small RNAs produced by the host},

author = {Eric Roberto Guimarães Rocha Aguiar and Roenick Proveti Olmo and Simona Paro and Flavia Viana Ferreira and Isaque João Silva da de Faria and Yaovi Mathias Honore Todjro and Francisco Pereira Lobo and Erna Geessien Kroon and Carine Meignin and Derek Gatherer and Jean-Luc Imler and João Trindade Marques},

url = {http://nar.oxfordjournals.org/lookup/doi/10.1093/nar/gkv587},

doi = {10.1093/nar/gkv587},

issn = {1362-4962},

year  = {2015},

date = {2015-07-01},

journal = {Nucleic Acids Research},

volume = {43},

number = {13},

pages = {6191--6206},

abstract = {Virus surveillance in vector insects is potentially of great benefit to public health. Large-scale sequencing of small and long RNAs has previously been used to detect viruses, but without any formal comparison of different strategies. Furthermore, the identification of viral sequences largely depends on similarity searches against reference databases. Here, we developed a sequence-independent strategy based on virus-derived small RNAs produced by the host response, such as the RNA interference pathway. In insects, we compared sequences of small and long RNAs, demonstrating that viral sequences are enriched in the small RNA fraction. We also noted that the small RNA size profile is a unique signature for each virus and can be used to identify novel viral sequences without known relatives in reference databases. Using this strategy, we characterized six novel viruses in the viromes of laboratory fruit flies and wild populations of two insect vectors: mosquitoes and sandflies. We also show that the small RNA profile could be used to infer viral tropism for ovaries among other aspects of virus biology. Additionally, our results suggest that virus detection utilizing small RNAs can also be applied to vertebrates, although not as efficiently as to plants and insects.},

keywords = {Animals, Contig Mapping, Female, imler, insects, M3i, meignin, Ovary, Plants, RNA, Sequence Analysis, Small Untranslated, Vertebrates, Viral, Viral Tropism, viruses},

pubstate = {published},

tppubtype = {article}

}

@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}

}

@article{taguchi_novel_1998,

title = {A novel insect defensin from the ant Formica rufa},

author = {S Taguchi and Philippe Bulet and Jules A Hoffmann},

issn = {0300-9084},

year  = {1998},

date = {1998-04-01},

journal = {Biochimie},

volume = {80},

number = {4},

pages = {343--346},

abstract = {By combination of size exclusion and reversed-phase chromatography, we have isolated a novel member of insect defensin-type antimicrobial peptides from the entire bodies of bacteria-challenged Formica rufa (hymenoptera, formicidae). The molecular mass of the purified peptide was estimated to be 4120.42 by matrix-assisted laser desorption/ionization-time of flight/mass spectrometry. Sequence analysis revealed that this peptide consisted of 40 amino acid residues with six cysteines engaged in the formation of three intramolecular disulfide bridges. This peptide is unique among the arthropod defensins in terms of the presence of asparatic acid and alanine at position 33 and as C-terminal residue, respectively. In addition, this novel defensin from Formica rufa has the particularity to have no C-terminal extension in contrast to those reported for other hymenoptera defensins.},

keywords = {Amino Acid, Animals, Anti-Bacterial Agents, Ants, Chromatography, High Pressure Liquid, hoffmann, Insect Proteins, insects, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Structure, Secondary, Sequence Alignment, Sequence Homology, Spectrometry},

pubstate = {published},

tppubtype = {article}

}

@article{hoffmann_innate_1996,

title = {Innate immunity in higher insects},

author = {Jules A Hoffmann and Jean-Marc Reichhart and Charles Hetru},

issn = {0952-7915},

year  = {1996},

date = {1996-02-01},

journal = {Curr. Opin. Immunol.},

volume = {8},

number = {1},

pages = {8--13},

abstract = {The hallmark of the innate immune response of higher insects is the rapid and transient synthesis of a battery of broad spectrum antimicrobial peptides by the fat body. The control of the genes encoding these peptides involves cis-regulatory promoter elements homologous to sequences functional in mammalian acute-phase genes. Study of immune-deficient mutants of Drosophila has indicated that distinct pathways control the antibacterial and antifungal responses in this species. Novel receptors potentially involved in the initiation of the immune response have been recently characterized.},

keywords = {Animals, Base Sequence, Cyclic, hoffmann, Immunity, Immunologic, Immunological, Innate, insects, M3i, Models, Peptide Hydrolases, Peptides, Receptors, reichhart},

pubstate = {published},

tppubtype = {article}

}

@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}

}

@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}

}

@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}

}

@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}

}

@article{hoffmann_chinless_1991,

title = {Chinless wonders. Molecular Aspects of Invertebrate Hormones. A Jacques Monod Conference sponsored by the Centre National de la Recherche Scientifique, Roscoff, France, October 14-19, 1990},

author = {Jules A Hoffmann and J Joosse},

issn = {1043-4674},

year  = {1991},

date = {1991-04-01},

journal = {New Biol.},

volume = {3},

number = {4},

pages = {336--340},

keywords = {Animals, Crustacea, Ecdysone, hoffmann, insects, Invertebrate Hormones, Juvenile Hormones, M3i, Neuropeptides, Receptors, Snails, Steroid},

pubstate = {published},

tppubtype = {article}

}

@article{hoffmann_cellular_1990,

title = {Cellular and molecular aspects of insect immunity},

author = {Danièle Hoffmann and Jules A Hoffmann},

issn = {0923-2494},

year  = {1990},

date = {1990-12-01},

journal = {Res. Immunol.},

volume = {141},

number = {9},

pages = {895--896},

keywords = {Animals, Cellular, hoffmann, Immunity, insects, M3i, Molecular Biology},

pubstate = {published},

tppubtype = {article}

}

@article{brehelin_comparative_1978,

title = {A comparative ultrastructural study of blood cells from nine insect orders},

author = {M Brehélin and Daniel Zachary and Jules A Hoffmann},

issn = {0302-766X},

year  = {1978},

date = {1978-01-01},

journal = {Cell Tissue Res.},

volume = {195},

number = {1},

pages = {45--57},

abstract = {An ultrastructural study of hemocytes from 9 different insect orders has led to the identification of 8 cell types: (1) Plasmatocytes, whose cytoplasm is filled with small dense lysosomes and large heterogeneous structures, are phagocytic cells. (2) Granulocytes, filled with uniformly electron dense granules, are involved in capsule formation. (3) Coagulocytes, which contain granules and structured globules and which possess a well developed RER, are involved in phagocytosis. (4) Spherule cells are filled with large spherical inclusions. (5) Oenocytoids are large cells with few cytoplasmic organelles. These 5 hemocyte types represent the majority of insect blood cells. (6) Prohemocytes, blastic cells which are one of the stem cells a hemocytes, are very few in number in each species investigated. (7) Thrombocytoids and (8) Prodocytes are restricted to a small number of insect species. The ultrastructural characteristics of these hemocyte types are discussed.},

keywords = {Animals, Blood Cells, Electron, Granulocytes, Hemocytes, hoffmann, insects, M3i, Microscopy, Species Specificity},

pubstate = {published},

tppubtype = {article}

}

@article{hoffmann_endocrine_1970,

title = {Endocrine regulation of production and differentiation of hemocytes in an orthopteran insect: Locusta migratoria migratoroides},

author = {Jules A Hoffmann},

issn = {0016-6480},

year  = {1970},

date = {1970-10-01},

journal = {Gen. Comp. Endocrinol.},

volume = {15},

number = {2},

pages = {198--219},

keywords = {Animals, Biological, Blood Cells, Electrocoagulation, Female, Hemolymph, hoffmann, insects, M3i, Male, Metamorphosis, Microscopy, Neurosecretory Systems, Phase-Contrast},

pubstate = {published},

tppubtype = {article}

}

@article{hoffmann_localization_1970,

title = {On the localization of phenol-oxidase activity in coagulocytes of Locusta migratoria L. (Orthoptera)},

author = {Jules A Hoffmann and A Porte and P Joly},

year  = {1970},

date = {1970-01-01},

journal = {C.R. Hebd. Seances Acad. Sci., Ser. D, Sci. Nat.},

volume = {270},

number = {4},

pages = {629--631},

keywords = {Animals, Catechol Oxidase, Hemolymph, hoffmann, insects, M3i, Tanning},

pubstate = {published},

tppubtype = {article}

}