Volohonsky Gloria, Hopp Ann-Katrin, Saenger Mélanie, Soichot Julien, Scholze Heidi, Boch Jens, Blandin Stéphanie A, Marois Eric
Transgenic Expression of the Anti-parasitic Factor TEP1 in the Malaria Mosquito Anopheles gambiae Article de journal
Dans: PLOS Pathogens, vol. 13, no. 1, p. e1006113, 2017, ISSN: 1553-7374.
Liens | BibTeX | Étiquettes: Anopheles gambiae, anti-parasitic factor, blandin, M3i, Malaria, marois, TEP1, transgenic
@article{volohonsky_transgenic_2017,
title = {Transgenic Expression of the Anti-parasitic Factor TEP1 in the Malaria Mosquito Anopheles gambiae},
author = {Gloria Volohonsky and Ann-Katrin Hopp and Mélanie Saenger and Julien Soichot and Heidi Scholze and Jens Boch and Stéphanie A Blandin and Eric Marois},
editor = {Kenneth D Vernick},
url = {http://dx.plos.org/10.1371/journal.ppat.1006113},
doi = {10.1371/journal.ppat.1006113},
issn = {1553-7374},
year = {2017},
date = {2017-01-01},
urldate = {2017-02-01},
journal = {PLOS Pathogens},
volume = {13},
number = {1},
pages = {e1006113},
keywords = {Anopheles gambiae, anti-parasitic factor, blandin, M3i, Malaria, marois, TEP1, transgenic},
pubstate = {published},
tppubtype = {article}
}
Pompon Julien, Levashina Elena A
A New Role of the Mosquito Complement-like Cascade in Male Fertility in Anopheles gambiae Article de journal
Dans: PLoS Biology, vol. 13, no. 9, p. e1002255, 2015.
Résumé | Liens | BibTeX | Étiquettes: Anopheles gambiae, TEP1
@article{J2015,
title = {A New Role of the Mosquito Complement-like Cascade in Male Fertility in Anopheles gambiae},
author = {Julien Pompon and Elena A Levashina},
url = {http://www.ncbi.nlm.nih.gov/pubmed/26394016},
year = {2015},
date = {2015-09-22},
journal = {PLoS Biology},
volume = {13},
number = {9},
pages = {e1002255},
abstract = {Thioester-containing protein 1 (TEP1) is a key immune factor that determines mosquito resistance to a wide range of pathogens, including malaria parasites. Here we report a new allele-specific function of TEP1 in male fertility. We demonstrate that during spermatogenesis TEP1 binds to and removes damaged cells through the same complement-like cascade that kills malaria parasites in the mosquito midgut. Further, higher fertility rates are mediated by an allele that renders the mosquito susceptible to Plasmodium. By elucidating the molecular and genetic mechanisms underlying TEP1 function in spermatogenesis, our study suggests that pleiotropic antagonism between reproduction and immunity may shape resistance of mosquito populations to malaria parasites.},
keywords = {Anopheles gambiae, TEP1},
pubstate = {published},
tppubtype = {article}
}
Buresova V, Hajdusek Ondrej, Franta Z, Loosova G, Grunclova L, Levashina Elena A, Kopacek P
Functional genomics of tick thioester-containing proteins reveal the ancient origin of the complement system Article de journal
Dans: J Innate Immun., vol. 3, no. 6, p. 623-30, 2011.
Résumé | BibTeX | Étiquettes: TEP1
@article{V2011,
title = {Functional genomics of tick thioester-containing proteins reveal the ancient origin of the complement system},
author = {V Buresova and Ondrej Hajdusek and Z Franta and G Loosova and L Grunclova and Elena A Levashina and P Kopacek},
year = {2011},
date = {2011-06-30},
journal = {J Innate Immun.},
volume = {3},
number = {6},
pages = {623-30},
abstract = {Ticks are important ectoparasites and vectors of multiple human and animal diseases. The obligatory hemophagy of ticks provides a formidable route for parasite transmission from one host to another. Parasite survival inside the tick relies on the ability of a pathogen to escape or inhibit tick immune defenses, but the molecular interactions between the tick and its pathogens remain poorly understood. Here we report that tick genomes are unique in that they contain all known classes of the α(2)-macroglobulin family (α(2)M-F) proteins: α(2)-macroglobulin pan-protease inhibitors, C3 complement components, and insect thioester-containing and macroglobulin-related proteins. By using RNA interference-mediated gene silencing in the hard tick Ixodes ricinus we demonstrated the central role of a C3-like molecule in the phagocytosis of bacteria and revealed nonredundant functions for α(2)M-F proteins. Assessment of α(2)M-F functions in a single organism should significantly contribute to the general knowledge on the evolution and function of the complement system. Importantly, understanding the tick immune mechanisms should provide new concepts for efficient transmission blocking of tick-borne diseases.},
keywords = {TEP1},
pubstate = {published},
tppubtype = {article}
}
Blandin Stéphanie A, Wang-Sattler R, Lamacchia Marina, Gagneur Julien, Lycett G, Ning Y, Levashina Elena A, Steinmetz Lars M
Dissecting the genetic basis of resistance to malaria parasites in Anopheles gambiae Article de journal
Dans: Science, vol. 326, no. 5949, p. 147-50, 2009.
Résumé | Liens | BibTeX | Étiquettes: blandin, M3i, TEP1
@article{SA2009,
title = {Dissecting the genetic basis of resistance to malaria parasites in Anopheles gambiae},
author = {Stéphanie A Blandin and R Wang-Sattler and Marina Lamacchia and Julien Gagneur and G Lycett and Y Ning and Elena A Levashina and Lars M Steinmetz},
url = {http://www.ncbi.nlm.nih.gov/pubmed/19797663},
year = {2009},
date = {2009-10-02},
journal = {Science},
volume = {326},
number = {5949},
pages = {147-50},
abstract = {The ability of Anopheles gambiae mosquitoes to transmit Plasmodium parasites is highly variable between individuals. However, the genetic basis of this variability has remained unknown. We combined genome-wide mapping and reciprocal allele-specific RNA interference (rasRNAi) to identify the genomic locus that confers resistance to malaria parasites and demonstrated that polymorphisms in a single gene encoding the antiparasitic thioester-containing protein 1 (TEP1) explain a substantial part of the variability in parasite killing. The link between TEP1 alleles and resistance to malaria may offer new tools for controlling malaria transmission. The successful application of rasRNAi in Anopheles suggests that it could also be applied to other organisms where RNAi is feasible to dissect complex phenotypes to the level of individual quantitative trait alleles.},
keywords = {blandin, M3i, TEP1},
pubstate = {published},
tppubtype = {article}
}
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 Article de journal
Dans: Cell Host Microbe, vol. 5, no. 3, p. 273–284, 2009, ISSN: 1934-6069.
Résumé | Liens | BibTeX | Étiquettes: 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}
}
Blandin Stéphanie A, Marois Eric, Levashina Elena A
Antimalarial responses in Anopheles gambiae: from a complement-like protein to a complement-like pathway Article de journal
Dans: Cell Host Microbe., vol. 3, no. 6, p. 364-74, 2008.
Résumé | Liens | BibTeX | Étiquettes: blandin, M3i, marois, TEP1
@article{SA2008,
title = {Antimalarial responses in Anopheles gambiae: from a complement-like protein to a complement-like pathway},
author = {Stéphanie A Blandin and Eric Marois and Elena A Levashina},
url = {http://www.ncbi.nlm.nih.gov/pubmed/18541213},
year = {2008},
date = {2008-06-12},
journal = {Cell Host Microbe.},
volume = {3},
number = {6},
pages = {364-74},
abstract = {Malaria transmission between humans depends on the ability of Anopheles mosquitoes to support Plasmodium development. New perspectives in vector control are emerging from understanding the mosquito immune system, which plays critical roles in parasite recognition and killing. A number of factors controlling this process have been recently identified, and key among them is TEP1, a homolog of human complement factor C3 whose binding to the parasite surface targets it for subsequent killing. Here, we review our current knowledge of mosquito factors that respond to Plasmodium infection and elaborate on the activity and mode of action of the TEP1 complement-like pathway.},
keywords = {blandin, M3i, marois, TEP1},
pubstate = {published},
tppubtype = {article}
}
Baxter Richard H, Chang C I, Chelliah Y, Blandin Stéphanie A, Levashina Elena A, Deisenhofer J
Structural basis for conserved complement factor-like function in the antimalarial protein TEP1 Article de journal
Dans: Proc Natl Acad Sci U S A., vol. 104, no. 28, p. 11615-20, 2007.
Résumé | Liens | BibTeX | Étiquettes: blandin, M3i, TEP1
@article{RH2007,
title = {Structural basis for conserved complement factor-like function in the antimalarial protein TEP1},
author = {Richard H Baxter and C I Chang and Y Chelliah and Stéphanie A Blandin and Elena A Levashina and J Deisenhofer},
url = {http://www.ncbi.nlm.nih.gov/pubmed/17606907},
year = {2007},
date = {2007-07-10},
journal = {Proc Natl Acad Sci U S A.},
volume = {104},
number = {28},
pages = {11615-20},
abstract = {Thioester-containing proteins (TEPs) are a major component of the innate immune response of insects to invasion by bacteria and protozoa. TEPs form a distinct clade of a superfamily that includes the pan-protease inhibitors alpha(2)-macroglobulins and vertebrate complement factors. The essential feature of these proteins is a sequestered thioester bond that, after cleavage in a protease-sensitive region of the protein, is activated and covalently binds to its target. Recently, TEP1 from the malarial vector Anopheles gambiae was shown to mediate recognition and killing of ookinetes from the malarial parasite Plasmodium berghei, a model for the human malarial parasite Plasmodium falciparum. Here, we present the crystal structure of the TEP1 isoform TEP1r. Although the overall protein fold of TEP1r resembles that of complement factor C3, the TEP1r domains are repositioned to stabilize the inactive conformation of the molecule (containing an intact thioester) in the absence of the anaphylotoxin domain, a central component of complement factors. The structure of TEP1r provides a molecular basis for the differences between TEP1 alleles TEP1r and TEP1s, which correlate with resistance of A. gambiae to infection by P. berghei.},
keywords = {blandin, M3i, TEP1},
pubstate = {published},
tppubtype = {article}
}
Blandin Stéphanie A, Levashina Elena A
Thioester-containing proteins in insect immunity Article de journal
Dans: Mol Immunol., vol. 40, no. 12, p. 903-8, 2004.
Résumé | BibTeX | Étiquettes: blandin, M3i, TEP1
@article{S2004b,
title = {Thioester-containing proteins in insect immunity},
author = {Stéphanie A Blandin and Elena A Levashina},
year = {2004},
date = {2004-02-01},
journal = {Mol Immunol.},
volume = {40},
number = {12},
pages = {903-8},
abstract = {Here, we discuss the role of thioester-containing proteins in innate immune responses of insects. TEPs are represented by multi-member families both in the fruitfly, Drosophila melanogaster, and in the mosquito, Anopheles gambiae. Phylogenetic analysis of the family suggests that in these two dipteran species evolution of TEPs followed independent scenarios as a result of specific adaptation to distinct ecological environments. Research on these two relatively simple model systems, which lack adaptive immunity, may provide new insights into the evolutionary origins and functions of this important protein family.},
keywords = {blandin, M3i, TEP1},
pubstate = {published},
tppubtype = {article}
}