Publications
2001
Michel T, Reichhart Jean-Marc, Hoffmann Jules A, Royet Julien
Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein Article de journal
Dans: Nature, vol. 414, no. 6865, p. 756–759, 2001, ISSN: 0028-0836.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid, Animals, Anti-Bacterial Agents, Anti-Infective Agents, Bacillus thuringiensis, Carrier Proteins, Cell Surface, Chromosome Mapping, Enterococcus faecalis, Fungi, Genes, Gram-Positive Bacteria, Hemolymph, hoffmann, Humans, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Micrococcus luteus, Mutation, Receptors, reichhart, Sequence Homology, Toll-Like Receptors
@article{michel_drosophila_2001,
title = {Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein},
author = {T Michel and Jean-Marc Reichhart and Jules A Hoffmann and Julien Royet},
doi = {10.1038/414756a},
issn = {0028-0836},
year = {2001},
date = {2001-12-01},
journal = {Nature},
volume = {414},
number = {6865},
pages = {756--759},
abstract = {Microbial infection activates two distinct intracellular signalling cascades in the immune-responsive fat body of Drosophila. Gram-positive bacteria and fungi predominantly induce the Toll signalling pathway, whereas Gram-negative bacteria activate the Imd pathway. Loss-of-function mutants in either pathway reduce the resistance to corresponding infections. Genetic screens have identified a range of genes involved in these intracellular signalling cascades, but how they are activated by microbial infection is largely unknown. Activation of the transmembrane receptor Toll requires a proteolytically cleaved form of an extracellular cytokine-like polypeptide, Spätzle, suggesting that Toll does not itself function as a bona fide recognition receptor of microbial patterns. This is in apparent contrast with the mammalian Toll-like receptors and raises the question of which host molecules actually recognize microbial patterns to activate Toll through Spätzle. Here we present a mutation that blocks Toll activation by Gram-positive bacteria and significantly decreases resistance to this type of infection. The mutation semmelweis (seml) inactivates the gene encoding a peptidoglycan recognition protein (PGRP-SA). Interestingly, seml does not affect Toll activation by fungal infection, indicating the existence of a distinct recognition system for fungi to activate the Toll pathway.},
keywords = {Amino Acid, Animals, Anti-Bacterial Agents, Anti-Infective Agents, Bacillus thuringiensis, Carrier Proteins, Cell Surface, Chromosome Mapping, Enterococcus faecalis, Fungi, Genes, Gram-Positive Bacteria, Hemolymph, hoffmann, Humans, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Micrococcus luteus, Mutation, Receptors, reichhart, Sequence Homology, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
1977
Hoffmann Danièle, Brehelin M, Hoffmann Jules A
First results of the antibacterial defense reactions of Locusta migratoria larva and imago Article de journal
Dans: Ann Parasitol Hum Comp, vol. 52, no. 1, p. 87–88, 1977, ISSN: 0003-4150.
BibTeX | Étiquettes: Animals, Bacillus thuringiensis, bacteria, Cellular, Grasshoppers, Hematopoietic System, Hemocytes, Hemolymph, hoffmann, Immunity, Larva, M3i, Muramidase
@article{hoffmann_first_1977,
title = {First results of the antibacterial defense reactions of Locusta migratoria larva and imago},
author = {Danièle Hoffmann and M Brehelin and Jules A Hoffmann},
issn = {0003-4150},
year = {1977},
date = {1977-02-01},
journal = {Ann Parasitol Hum Comp},
volume = {52},
number = {1},
pages = {87--88},
keywords = {Animals, Bacillus thuringiensis, bacteria, Cellular, Grasshoppers, Hematopoietic System, Hemocytes, Hemolymph, hoffmann, Immunity, Larva, M3i, Muramidase},
pubstate = {published},
tppubtype = {article}
}