André Christophe, Veillard Florian, Wolff Philippe, Lobstein Anne-marie, Compain Guillaume, Monsarrat Clément, Reichhart Jean-marc, Noûs Camille, Burnouf Dominique, Guichard Gilles, Wagner Jerome
Antibacterial activity of a dual peptide targeting the Escherichia coli sliding clamp and the ribosome Article de journal
Dans: RSC Chemical Biology, vol. 1, no. 3, p. 137-147, 2020.
Résumé | Liens | BibTeX | Étiquettes: Antibacterial, Antimicrobial peptides, Bacterial, clamp, E. coli, M3i, reichhart
@article{veillard2020,
title = {Antibacterial activity of a dual peptide targeting the Escherichia coli sliding clamp and the ribosome},
author = {Christophe André and Florian Veillard and Philippe Wolff and Anne-marie Lobstein and Guillaume Compain and Clément Monsarrat and Jean-marc Reichhart and Camille Noûs and Dominique Burnouf and Gilles Guichard and Jerome Wagner },
url = {https://pubs.rsc.org/en/content/articlelanding/2020/CB/D0CB00060D#!divAbstract},
doi = {10.1039/D0CB00060D},
year = {2020},
date = {2020-07-16},
journal = {RSC Chemical Biology},
volume = {1},
number = {3},
pages = {137-147},
abstract = {The bacterial processivity factor, or sliding clamp (SC), is a target of choice for new antibacterial drugs development. We have previously developed peptides that target Escherichia coli SC and block its interaction with DNA polymerases in vitro. Here, one such SC binding peptide was fused to a Proline-rich AntiMicrobial Peptide (PrAMP) to allow its internalization into E. coli cells. Co-immunoprecipitation assays with a N-terminally modified bifunctional peptide that still enters the bacteria but fails to interact with the bacterial ribosome, the major target of PrAMPs, demonstrate that it actually interacts with the bacterial SC. Moreover, when compared to SC non-binding controls, this peptide induces a ten-fold higher antibacterial activity against E. coli, showing that the observed antimicrobial activity is linked to SC binding. Finally, an unmodified bifunctional compound significantly increases the survival of Drosophila melanogaster flies challenged by an E. coli infection. Our study demonstrates the potential of PrAMPs to transport antibiotics into the bacterial cytoplasm and validates the development of drugs targeting the bacterial processivity factor of Gram-negative bacteria as a promising new class of antibiotics.},
keywords = {Antibacterial, Antimicrobial peptides, Bacterial, clamp, E. coli, M3i, reichhart},
pubstate = {published},
tppubtype = {article}
}
Imler Jean-Luc
Overview of Drosophila immunity: a historical perspective Article de journal
Dans: Developmental and Comparative Immunology, vol. 42, no. 1, p. 3–15, 2014, ISSN: 1879-0089.
Résumé | Liens | BibTeX | Étiquettes: Allergy and Immunology, Animal, Animals, Antimicrobial Cationic Peptides, Antimicrobial peptides, history, Humans, IMD pathway, imler, Immunity, Innate, innate immunity, M3i, Models, Pattern recognition receptors, Signal Transduction, Toll-Like Receptors
@article{imler_overview_2014,
title = {Overview of Drosophila immunity: a historical perspective},
author = {Jean-Luc Imler},
doi = {10.1016/j.dci.2013.08.018},
issn = {1879-0089},
year = {2014},
date = {2014-01-01},
journal = {Developmental and Comparative Immunology},
volume = {42},
number = {1},
pages = {3--15},
abstract = {The functional analysis of genes from the model organism Drosophila melanogaster has provided invaluable information for many cellular and developmental or physiological processes, including immunity. The best-understood aspect of Drosophila immunity is the inducible humoral response, first recognized in 1972. This pioneering work led to a remarkable series of findings over the next 30 years, ranging from the identification and characterization of the antimicrobial peptides produced, to the deciphering of the signalling pathways activating the genes that encode them and, ultimately, to the discovery of the receptors sensing infection. These studies on an insect model coincided with a revival of the field of innate immunity, and had an unanticipated impact on the biomedical field.},
keywords = {Allergy and Immunology, Animal, Animals, Antimicrobial Cationic Peptides, Antimicrobial peptides, history, Humans, IMD pathway, imler, Immunity, Innate, innate immunity, M3i, Models, Pattern recognition receptors, Signal Transduction, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}