Publications
2011
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 Article de journal
Dans: PLoS ONE, vol. 6, no. 3, p. e14743, 2011, ISSN: 1932-6203.
Résumé | Liens | BibTeX | Étiquettes: 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}
}
2004
Bischoff Vincent, Vignal Cécile, Boneca Ivo G, Michel Tatiana, Hoffmann Jules A, Royet Julien
Function of the drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria Article de journal
Dans: Nat. Immunol., vol. 5, no. 11, p. 1175–1180, 2004, ISSN: 1529-2908.
Résumé | Liens | BibTeX | Étiquettes: Animals, Carrier Proteins, Cell Surface, Gram-Positive Bacteria, Gram-Positive Bacterial Infections, hoffmann, M3i, Mutation, Mycoses, Receptors, Staphylococcus aureus, Toll-Like Receptors
@article{bischoff_function_2004,
title = {Function of the drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria},
author = {Vincent Bischoff and Cécile Vignal and Ivo G Boneca and Tatiana Michel and Jules A Hoffmann and Julien Royet},
doi = {10.1038/ni1123},
issn = {1529-2908},
year = {2004},
date = {2004-11-01},
journal = {Nat. Immunol.},
volume = {5},
number = {11},
pages = {1175--1180},
abstract = {The activation of an immune response requires recognition of microorganisms by host receptors. In drosophila, detection of Gram-positive bacteria is mediated by cooperation between the peptidoglycan-recognition protein-SA (PGRP-SA) and Gram-negative binding protein 1 (GNBP1) proteins. Here we show that some Gram-positive bacterial species activate an immune response in a PGRP-SA- and GNBP1-independent manner, indicating that alternative receptors exist. Consistent with this, we noted that PGRP-SD mutants were susceptible to some Gram-positive bacteria and that a loss-of-function mutation in PGRP-SD severely exacerbated the PGRP-SA and GNBP1 mutant phenotypes. These data indicate that PGRP-SD can function as a receptor for Gram-positive bacteria and shows partial redundancy with the PGRP-SA-GNBP1 complex.},
keywords = {Animals, Carrier Proteins, Cell Surface, Gram-Positive Bacteria, Gram-Positive Bacterial Infections, hoffmann, M3i, Mutation, Mycoses, Receptors, Staphylococcus aureus, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
2002
Pantarotto Davide, Bianco Alberto, Pellarini Federica, Tossi Alessandro, Giangaspero Anna, Zelezetsky Igor, Briand Jean-Paul, Prato Maurizio
Solid-phase synthesis of fullerene-peptides Article de journal
Dans: Journal of the American Chemical Society, vol. 124, no. 42, p. 12543–12549, 2002, ISSN: 0002-7863.
Résumé | Liens | BibTeX | Étiquettes: Amino Acids, Anti-Bacterial Agents, Anti-Infective Agents, Candida albicans, Electrospray Ionization, Enkephalin, Escherichia coli, Fluorenes, Fullerenes, I2CT, Leucine, Mass, Microbial Sensitivity Tests, Oligopeptides, Spectrometry, Staphylococcus aureus, Team-Bianco
@article{pantarotto_solid-phase_2002,
title = {Solid-phase synthesis of fullerene-peptides},
author = {Davide Pantarotto and Alberto Bianco and Federica Pellarini and Alessandro Tossi and Anna Giangaspero and Igor Zelezetsky and Jean-Paul Briand and Maurizio Prato},
doi = {10.1021/ja027603q},
issn = {0002-7863},
year = {2002},
date = {2002-10-01},
journal = {Journal of the American Chemical Society},
volume = {124},
number = {42},
pages = {12543--12549},
abstract = {The solid-phase synthesis of peptides (SPPS) containing [60]fullerene-functionalized amino acids is reported. A new amino acid, fulleropyrrolidino-glutamic acid (Fgu), is used for the SPPS of a series of analogues of different length based on the natural Leu(5)-Enkephalin and on cationic antimicrobial peptides. These fullero-peptides were prepared on different solid supports to analyze the influence of the resin on the synthesis. Optimized protocols for the coupling and deprotection procedures were determined allowing the synthesis of highly pure peptides in sufficient quantities for evaluation of biological activities. In particular, to avoid side reactions of the fullerene moiety with bases and nucleophiles, the removal of the protecting groups was performed under inert conditions (nitrogen or argon in the dark). We have encountered serious problems with the recovery of the crude compounds, especially when Fgu was inserted in the proximity of the resin core as fullero-peptides tend to remain embedded inside the resin. Eventually, all of the fullero-peptides were easily purified, and the cationic peptides were tested for their antimicrobial activities. They displayed a specific activity against the Gram-positive bacterium S. aureus and also lysed erythrocytes. The availability of a fullero-amino acid easily useable in the SPPS of fullero-peptides may thus open the way to the synthesis of new types of biologically active oligomers.},
keywords = {Amino Acids, Anti-Bacterial Agents, Anti-Infective Agents, Candida albicans, Electrospray Ionization, Enkephalin, Escherichia coli, Fluorenes, Fullerenes, I2CT, Leucine, Mass, Microbial Sensitivity Tests, Oligopeptides, Spectrometry, Staphylococcus aureus, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}