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2009
Partidos Charalambos D, Hoebeke Johan, Wieckowski Sébastien, Chaloin Olivier, Bianco Alberto, Moreau Emmanuel, Briand Jean-Paul, Desgranges Claude, Muller Sylviane
Immunomodulatory consequences of ODN CpG-polycation complexes Journal Article
In: Methods (San Diego, Calif.), vol. 49, no. 4, pp. 328–333, 2009, ISSN: 1095-9130.
Abstract | Links | BibTeX | Tags: Animals, carbon, CpG Islands, Humans, I2CT, Immunologic Factors, Nanotubes, Oligodeoxyribonucleotides, Polyamines, Team-Bianco, Transcriptional Activation
@article{partidos_immunomodulatory_2009,
title = {Immunomodulatory consequences of ODN CpG-polycation complexes},
author = {Charalambos D Partidos and Johan Hoebeke and Sébastien Wieckowski and Olivier Chaloin and Alberto Bianco and Emmanuel Moreau and Jean-Paul Briand and Claude Desgranges and Sylviane Muller},
doi = {10.1016/j.ymeth.2009.03.005},
issn = {1095-9130},
year = {2009},
date = {2009-12-01},
journal = {Methods (San Diego, Calif.)},
volume = {49},
number = {4},
pages = {328--333},
abstract = {Immunostimulatory ODN CpGs have extensively been tested as adjuvants and immunotherapeutics and hold a lot of promise for human use. In our studies we took advantage of their negative charge to study their biological activities after being complexed with carbon nanotubes, a novel vector for vaccine delivery and Tat protein of HIV, a target protein for therapeutic or prophylactic intervention. In the case of carbon nanotubes, ODN CpGs were able to form stable complexes based on charge interaction and exert increased immunostimulatory activity in vitro. With regard to the Tat protein, ODN CpGs were shown to bind effectively through the basic domain of the protein representing residues 44-61. Moreover, using surface Plasmon Resonance Technology and an in vitro cellular system, ODN CpGs were shown to inhibit the interaction of Tat protein with the transactivation responsive element, a bulged RNA hairpin structure. However, when ODN CpGs were complexed with Tat they readily increased the apoptotic properties of this protein as studied in CD3-stimulated Jurkat cells. Overall, our findings together with published data support the view that for harnessing the beneficial effects of ODN CpGs a careful consideration has to be given depending on the target intervention.},
keywords = {Animals, carbon, CpG Islands, Humans, I2CT, Immunologic Factors, Nanotubes, Oligodeoxyribonucleotides, Polyamines, Team-Bianco, Transcriptional Activation},
pubstate = {published},
tppubtype = {article}
}
Immunostimulatory ODN CpGs have extensively been tested as adjuvants and immunotherapeutics and hold a lot of promise for human use. In our studies we took advantage of their negative charge to study their biological activities after being complexed with carbon nanotubes, a novel vector for vaccine delivery and Tat protein of HIV, a target protein for therapeutic or prophylactic intervention. In the case of carbon nanotubes, ODN CpGs were able to form stable complexes based on charge interaction and exert increased immunostimulatory activity in vitro. With regard to the Tat protein, ODN CpGs were shown to bind effectively through the basic domain of the protein representing residues 44-61. Moreover, using surface Plasmon Resonance Technology and an in vitro cellular system, ODN CpGs were shown to inhibit the interaction of Tat protein with the transactivation responsive element, a bulged RNA hairpin structure. However, when ODN CpGs were complexed with Tat they readily increased the apoptotic properties of this protein as studied in CD3-stimulated Jurkat cells. Overall, our findings together with published data support the view that for harnessing the beneficial effects of ODN CpGs a careful consideration has to be given depending on the target intervention.
Fraiture Malou, Baxter Richard H G, Steinert Stefanie, Chelliah Yogarany, Frolet Cécile, Quispe-Tintaya Wilber, Hoffmann Jules A, Blandin Stéphanie A, Levashina Elena A
Two mosquito LRR proteins function as complement control factors in the TEP1-mediated killing of Plasmodium Journal Article
In: Cell Host Microbe, vol. 5, no. 3, pp. 273–284, 2009, ISSN: 1934-6069.
Abstract | Links | BibTeX | Tags: Animals, Anopheles, APL1, Biological, blandin, Complement System Proteins, Hemolymph, hoffmann, Immunologic Factors, LRIM1, M3i, Models, Plasmodium, Protein Binding, Proteins, TEP1
@article{fraiture_two_2009,
title = {Two mosquito LRR proteins function as complement control factors in the TEP1-mediated killing of Plasmodium},
author = {Malou Fraiture and Richard H G Baxter and Stefanie Steinert and Yogarany Chelliah and Cécile Frolet and Wilber Quispe-Tintaya and Jules A Hoffmann and Stéphanie A Blandin and Elena A Levashina},
doi = {10.1016/j.chom.2009.01.005},
issn = {1934-6069},
year = {2009},
date = {2009-03-01},
journal = {Cell Host Microbe},
volume = {5},
number = {3},
pages = {273--284},
abstract = {Plasmodium development within Anopheles mosquitoes is a vulnerable step in the parasite transmission cycle, and targeting this step represents a promising strategy for malaria control. The thioester-containing complement-like protein TEP1 and two leucine-rich repeat (LRR) proteins, LRIM1 and APL1, have been identified as major mosquito factors that regulate parasite loads. Here, we show that LRIM1 and APL1 are required for binding of TEP1 to parasites. RNAi silencing of the LRR-encoding genes results in deposition of TEP1 on Anopheles tissues, thereby depleting TEP1 from circulation in the hemolymph and impeding its binding to Plasmodium. LRIM1 and APL1 not only stabilize circulating TEP1, they also stabilize each other prior to their interaction with TEP1. Our results indicate that three major antiparasitic factors in mosquitoes jointly function as a complement-like system in parasite killing, and they reveal a role for LRR proteins as complement control factors.},
keywords = {Animals, Anopheles, APL1, Biological, blandin, Complement System Proteins, Hemolymph, hoffmann, Immunologic Factors, LRIM1, M3i, Models, Plasmodium, Protein Binding, Proteins, TEP1},
pubstate = {published},
tppubtype = {article}
}
Plasmodium development within Anopheles mosquitoes is a vulnerable step in the parasite transmission cycle, and targeting this step represents a promising strategy for malaria control. The thioester-containing complement-like protein TEP1 and two leucine-rich repeat (LRR) proteins, LRIM1 and APL1, have been identified as major mosquito factors that regulate parasite loads. Here, we show that LRIM1 and APL1 are required for binding of TEP1 to parasites. RNAi silencing of the LRR-encoding genes results in deposition of TEP1 on Anopheles tissues, thereby depleting TEP1 from circulation in the hemolymph and impeding its binding to Plasmodium. LRIM1 and APL1 not only stabilize circulating TEP1, they also stabilize each other prior to their interaction with TEP1. Our results indicate that three major antiparasitic factors in mosquitoes jointly function as a complement-like system in parasite killing, and they reveal a role for LRR proteins as complement control factors.
