I2CT

@article{matskevich_drosophila_2010b,

title = {The Drosophila PRR GNBP3 assembles effector complexes involved in antifungal defenses independently of its Toll-pathway activation function},

author = {Alexey A Matskevich and Jessica Quintin and Dominique Ferrandon},

doi = {10.1002/eji.200940164},

issn = {1521-4141},

year  = {2010},

date = {2010-05-01},

journal = {Eur. J. Immunol.},

volume = {40},

number = {5},

pages = {1244--1254},

abstract = {The Drosophila Toll-signaling pathway controls the systemic antifungal host response. Gram-negative binding protein 3 (GNBP3), a member of the beta-glucan recognition protein family senses fungal infections and activates this pathway. A second detection system perceives the activity of proteolytic fungal virulence factors and redundantly activates Toll. GNBP3(hades) mutant flies succumb more rapidly to Candida albicans and to entomopathogenic fungal infections than WT flies, despite normal triggering of the Toll pathway via the virulence detection system. These observations suggest that GNBP3 triggers antifungal defenses that are not dependent on activation of the Toll pathway. Here, we show that GNBP3 agglutinates fungal cells. Furthermore, it can activate melanization in a Toll-independent manner. Melanization is likely to be an essential defense against some fungal infections given that the entomopathogenic fungus Beauveria bassiana inhibits the activity of the main melanization enzymes, the phenol oxidases. Finally, we show that GNBP3 assembles "attack complexes", which comprise phenoloxidase and the necrotic serpin. We propose that Drosophila GNBP3 targets fungi immediately at the inception of the infection by bringing effector molecules in direct contact with the invading microorganisms.},

keywords = {Agglutination, Animals, Beauveria, Beauveria/immunology, Candida albicans, Candida albicans/immunology, Carrier Proteins, Carrier Proteins/*immunology/pharmacology, Drosophila melanogaster/*immunology/microbiology, Drosophila Proteins/*immunology/pharmacology/physiology, Enzyme Activation, ferrandon, Fungal, Fungi, Fungi/*immunology, Hemolymph, Hemolymph/immunology, M3i, Melanins, Melanins/*physiology, Monophenol Monooxygenase, Monophenol Monooxygenase/physiology, Multiprotein Complexes, Multiprotein Complexes/physiology, Recombinant Fusion Proteins, Recombinant Fusion Proteins/pharmacology, Serpins, Serpins/physiology, Spores, Toll-Like Receptors, Toll-Like Receptors/immunology},

pubstate = {published},

tppubtype = {article}

}

@article{zachary_role_1975,

title = {Role of the “thrombocytoids” in capsule formation in the dipteran Calliphora erythrocephala},

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

issn = {0302-766X},

year  = {1975},

date = {1975-10-01},

journal = {Cell Tissue Res.},

volume = {162},

number = {3},

pages = {343--348},

abstract = {Of the three hemocyte types present in the blood of Calliphora, only one participates in capsule formation around implanted cellophane. This hemocyte, the thrombocytoid, shows in the blood a tendency to dissociate into numerous small cytoplasmic fragments, comparable to the mammalian megakaryocyte. This tendency is dramatically increased during the process of encapsulation. Most of the intact thrombocytoids and the numerous fragments participating in capsule formation do not show any particular modifications in their cytoplasm during this process, which corresponds to a mere sequestration of the implant. Dense material, resulting from necrotic cell debris and hemolymph lipoproteins, is often observed between the cellophane and encapsulating thrombocytoids, which apparently participate in the resorption of this material.},

keywords = {Agglutination, Animals, Diptera, Foreign Bodies, Hemolymph, hoffmann, M3i, Phagocytosis},

pubstate = {published},

tppubtype = {article}

}