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David J Siveter - One of the best experts on this subject based on the ideXlab platform.
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a new phyllocarid Crustacea malacostraca from the silurian fossil lagerstatte of herefordshire uk
Proceedings of The Royal Society B: Biological Sciences, 2004Co-Authors: Derek E G Briggs, Mark D Sutton, David J SiveterAbstract:A new three-dimensionally preserved arthropod, Cinerocaris magnifica, from the Wenlock Series (Silurian) of Herefordshire, UK, is described and assigned to the Phyllocarida (Crustacea). The description and reconstruction are based on specimens that have been serially ground, reconstructed by computer and rendered in three dimensions as coloured virtual models. Cinerocaris magnifica displayed the tagmosis characteristic of phyllocarids, with eight thoracic and seven abdominal somites, terminating in a telson with furca. The remarkable preservation of the appendages makes this the earliest completely known malacostracan Crustacean. Two pairs of antennae (the first with two flagella) were followed by a mandible and first maxilla, each with a slender palp-like ramus. The second maxilla consisted of a limb stem with endites and an endopod that tapered distally. There was no exopod. The thoracopods comprised a limb stem with six or seven endites, an arrangement previously known only in entomostracans, and an endopod with about five endites. Flap-like outer rami correspond to an exopod and epipods. The pleopods bore two long slender oar-blade-like rami. Cladistic analysis places C. magnifica as a plesion within the Echinocaridina. It provides critical evidence of the limb morphology of an early malacostracan, which will be important in understanding Crustacean evolution.
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A new phyllocarid (Crustacea: Malacostraca) from the Silurian Fossil-Lagerstatte of Herefordshire, UK.
2004Co-Authors: De Briggs, David J SiveterAbstract:A new three-dimensionally preserved arthropod, Cinerocaris magnifica, from the Wenlock Series (Silurian) of Herefordshire, UK, is described and assigned to the Phyllocarida (Crustacea). The description and reconstruction are based on specimens that have been serially ground, reconstructed by computer and rendered in three dimensions as coloured virtual models. Cinerocaris magnifica displayed the tagmosis characteristic of phyllocarids, with eight thoracic and seven abdominal somites, terminating in a telson with furca. The remarkable preservation of the appendages makes this the earliest completely known malacostracan Crustacean. Two pairs of antennae (the first with two flagella) were followed by a mandible and first maxilla, each with a slender palp-like ramus. The second maxilla consisted of a limb stem with endites and an endopod that tapered distally. There was no exopod. The thoracopods comprised a limb stem with six or seven endites, an arrangement previously known only in entomostracans, and an endopod with about five endites. Flap-like outer rami correspond to an exopod and epipods. The pleopods bore two long slender oar-blade-like rami. Cladistic analysis places C. magnifica as a plesion within the Echinocaridina. It provides critical evidence of the limb morphology of an early malacostracan, which will be important in understanding Crustacean evolution
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Silurian Fossil-Lagerstätte of Herefordshire, UK
2003Co-Authors: Derek E G Briggs, Mark D Sutton, David J SiveterAbstract:A new three-dimensionally preserved arthropod, Cinerocaris magnifica, from the Wenlock Series (Silurian) of Herefordshire, UK, is described and assigned to the Phyllocarida (Crustacea). The description and reconstruction are based on specimens that have been serially ground, reconstructed by computer and rendered in three dimensions as coloured virtual models. Cinerocaris magnifica displayed the tagmosis characteristic of phyllocarids, with eight thoracic and seven abdominal somites, terminating in a telson with furca. The remarkable preservation of the appendages makes this the earliest completely known malacostracan Crustacean. Two pairs of antennae (the first with two flagella) were followed by a mandible and first maxilla, each with a slender palp-like ramus. The second maxilla consisted of a limb stem with endites and an endopod that tapered distally. There was no exopod. The thoracopods comprised a limb stem with six or seven endites, an arrangement previously known only in entomostracans, and an endopod with about five endites. Flap-like outer rami correspond to an exopod and epipods. The pleopods bore two long slender oar-blade-like rami. Cladistic analysis places C. magnifica as a plesion within the Echino-caridina. It provides critical evidence of the limb morphology of an early malacostracan, which will be important in understanding Crustacean evolution
Thomas Soin - One of the best experts on this subject based on the ideXlab platform.
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Cloning and functional analysis of the ecdysteroid receptor complex in the opossum shrimp Neomysis integer (Leach, 1814).
Aquatic Toxicology, 2013Co-Authors: R. De Wilde, Thomas Soin, Pierre Rouge, Olivier Christiaens, Colin R. Janssen, Guy SmaggheAbstract:a b s t r a c t In this paper, the non-target effects of tebufenozide were evaluated on the estuarine Crustacean, the opposum shrimp Neomysis integer (Leach, 1814). Tebufenozide is a synthetic non-steroidal ecdysone agonist insecticide and regarded as potential endocrine-disrupting chemical (EDC). N. integer is the most used Crustacean in ecotoxicological research in parallel to Daphnia sp. and has been proposed for the regulatory testing of potential EDCs in the US, Europe and Japan. Major results were: (i) cDNAs encoding the ecdysteroid receptor (EcR) and the retinoid-X-receptor (RXR), were cloned and sequenced, and subsequent molecular phylogenetic analysis (maximum likeli- hood and neighbor-joining) revealed that the amino acid sequence of the ligand binding domain (LBD) of N. integer EcR (NiEcR) clusters as an outgroup of the Crustacea, while NiRXR-LBD clusters in the Malacos- tracan clade (bootstrap percentage = 75%). (ii) 3D-modeling of ligand binding to NiEcR-LBD demonstrated an incompatibility of the insecticide tebufenozide to fit into the NiEcR-ligand binding pocket. This was in great contrast to ponasterone A (PonA) that is the natural molting hormone in Crustacea and for which efficient docking was demonstrated. In addition, the heterodimerization of NiEcR-LBD with the com- mon shrimp Crangon crangon (Linnaeus, 1758) RXR-LBD (CrcRXR-LBD) was also modeled in silico. (iii) With use of insect Hi5 cells, chimeric constructs of NiEcR-LBD and CrcRXR-LBD fused to either the yeast Gal4-DNA binding domain (DBD) or Gal4-activation domain (AD) were cloned into expression plasmids and co-transfected with a Gal4 reporter to quantify the protein-protein interactions of NiEcR-LBD with CrcRXR-LBD. Investigation of the ligand effect of PonA and tebufenozide revealed that only the presence of PonA could induce dimerization of this heterologous receptor complex. (iv) Finally, in an in vivo toxicity assay, N. integer juveniles were exposed to tebufenozide at a concentration of 100 g/L, and no effects against the molting process and nymphal development were scored.
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the brown shrimp crangon crangon l ecdysteroid receptor complex cloning structural modeling of the ligand binding domain and functional expression in an ecr deficient drosophila cell line
General and Comparative Endocrinology, 2010Co-Authors: Yves Verhaegen, Luc Swevers, K. Parmentier, Thomas Soin, Pierre Rouge, Wim De Coen, K. CooremanAbstract:cDNAs encoding ecdysteroid receptor (EcR) and retinoid X receptor (RXR) were cloned and sequenced from brown shrimp Crangon crangon (Crustacea: Decapoda), a common faunal species and commercially important in the North-West European coastal waters. A 3D model of the ligand-binding domain (LBD) of EcR was created and docking of ponasterone A (PonA) was simulated in silico. Finally, we report the transfection of expression plasmids for these receptors in the mutant Drosophila L57-3-11 cell line. Through an ecdysteroid responsive reporter assay we clearly prove the functionality of shrimp ecdysteroid receptor in the transfected L57-3-11 cell line. Our results indicate that the Drosophila L57-3-11 cell line and in silico LBD modeling can be used to study the function of Crustacean ecdysteroid receptors and be applied to assess endocrine disrupting effects on non-target Crustacean species.
Pierre Rouge - One of the best experts on this subject based on the ideXlab platform.
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Cloning and functional analysis of the ecdysteroid receptor complex in the opossum shrimp Neomysis integer (Leach, 1814).
Aquatic Toxicology, 2013Co-Authors: R. De Wilde, Thomas Soin, Pierre Rouge, Olivier Christiaens, Colin R. Janssen, Guy SmaggheAbstract:a b s t r a c t In this paper, the non-target effects of tebufenozide were evaluated on the estuarine Crustacean, the opposum shrimp Neomysis integer (Leach, 1814). Tebufenozide is a synthetic non-steroidal ecdysone agonist insecticide and regarded as potential endocrine-disrupting chemical (EDC). N. integer is the most used Crustacean in ecotoxicological research in parallel to Daphnia sp. and has been proposed for the regulatory testing of potential EDCs in the US, Europe and Japan. Major results were: (i) cDNAs encoding the ecdysteroid receptor (EcR) and the retinoid-X-receptor (RXR), were cloned and sequenced, and subsequent molecular phylogenetic analysis (maximum likeli- hood and neighbor-joining) revealed that the amino acid sequence of the ligand binding domain (LBD) of N. integer EcR (NiEcR) clusters as an outgroup of the Crustacea, while NiRXR-LBD clusters in the Malacos- tracan clade (bootstrap percentage = 75%). (ii) 3D-modeling of ligand binding to NiEcR-LBD demonstrated an incompatibility of the insecticide tebufenozide to fit into the NiEcR-ligand binding pocket. This was in great contrast to ponasterone A (PonA) that is the natural molting hormone in Crustacea and for which efficient docking was demonstrated. In addition, the heterodimerization of NiEcR-LBD with the com- mon shrimp Crangon crangon (Linnaeus, 1758) RXR-LBD (CrcRXR-LBD) was also modeled in silico. (iii) With use of insect Hi5 cells, chimeric constructs of NiEcR-LBD and CrcRXR-LBD fused to either the yeast Gal4-DNA binding domain (DBD) or Gal4-activation domain (AD) were cloned into expression plasmids and co-transfected with a Gal4 reporter to quantify the protein-protein interactions of NiEcR-LBD with CrcRXR-LBD. Investigation of the ligand effect of PonA and tebufenozide revealed that only the presence of PonA could induce dimerization of this heterologous receptor complex. (iv) Finally, in an in vivo toxicity assay, N. integer juveniles were exposed to tebufenozide at a concentration of 100 g/L, and no effects against the molting process and nymphal development were scored.
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the brown shrimp crangon crangon l ecdysteroid receptor complex cloning structural modeling of the ligand binding domain and functional expression in an ecr deficient drosophila cell line
General and Comparative Endocrinology, 2010Co-Authors: Yves Verhaegen, Luc Swevers, K. Parmentier, Thomas Soin, Pierre Rouge, Wim De Coen, K. CooremanAbstract:cDNAs encoding ecdysteroid receptor (EcR) and retinoid X receptor (RXR) were cloned and sequenced from brown shrimp Crangon crangon (Crustacea: Decapoda), a common faunal species and commercially important in the North-West European coastal waters. A 3D model of the ligand-binding domain (LBD) of EcR was created and docking of ponasterone A (PonA) was simulated in silico. Finally, we report the transfection of expression plasmids for these receptors in the mutant Drosophila L57-3-11 cell line. Through an ecdysteroid responsive reporter assay we clearly prove the functionality of shrimp ecdysteroid receptor in the transfected L57-3-11 cell line. Our results indicate that the Drosophila L57-3-11 cell line and in silico LBD modeling can be used to study the function of Crustacean ecdysteroid receptors and be applied to assess endocrine disrupting effects on non-target Crustacean species.
K. Cooreman - One of the best experts on this subject based on the ideXlab platform.
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the brown shrimp crangon crangon l ecdysteroid receptor complex cloning structural modeling of the ligand binding domain and functional expression in an ecr deficient drosophila cell line
General and Comparative Endocrinology, 2010Co-Authors: Yves Verhaegen, Luc Swevers, K. Parmentier, Thomas Soin, Pierre Rouge, Wim De Coen, K. CooremanAbstract:cDNAs encoding ecdysteroid receptor (EcR) and retinoid X receptor (RXR) were cloned and sequenced from brown shrimp Crangon crangon (Crustacea: Decapoda), a common faunal species and commercially important in the North-West European coastal waters. A 3D model of the ligand-binding domain (LBD) of EcR was created and docking of ponasterone A (PonA) was simulated in silico. Finally, we report the transfection of expression plasmids for these receptors in the mutant Drosophila L57-3-11 cell line. Through an ecdysteroid responsive reporter assay we clearly prove the functionality of shrimp ecdysteroid receptor in the transfected L57-3-11 cell line. Our results indicate that the Drosophila L57-3-11 cell line and in silico LBD modeling can be used to study the function of Crustacean ecdysteroid receptors and be applied to assess endocrine disrupting effects on non-target Crustacean species.
Petra H Lenz - One of the best experts on this subject based on the ideXlab platform.
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identification of chelicerate neuropeptides using bioinformatics of publicly accessible expressed sequence tags
General and Comparative Endocrinology, 2011Co-Authors: Andrew E Christie, Daniel H Nolan, Paul Ohno, Niko Hartline, Petra H LenzAbstract:While numerous investigations have focused on the identification of neuropeptides in arthropods, most have been conducted on members of the Hexapoda or Crustacea, and little is currently known about those in the Chelicerata. Here, publicly accessible expressed sequence tags (ESTs) were mined for putative chelicerate neuropeptide-encoding transcripts; the peptides encoded by the ESTs were deduced using on-line peptide prediction programs and homology to known isoforms. Fifty-eight ESTs representing eight peptide families/subfamilies were identified using this strategy. Of note was the prediction of the first authentic chelicerate C-type allatostatin, pQIRYHQCYFNPISCF, from the mite Tetranychus urticae, as well as the prediction a novel allatostatin CC peptide, GEGKMFWRCYFNAVSCF, from both the tick Amblyomma variegatum and the scorpion Mesobuthus gibbosus. Also identified from T. urticae were authentic Crustacean cardioactive peptide (CCAP), several peptides belonging to the Crustacean hyperglycemic hormone/ion transport peptide superfamily, members of the calcitonin-like diuretic hormone/diuretic hormone 31 family, and several FMRFamide-like peptides, specifically members of the neuropeptide F (NPF) and short neuropeptide F subfamilies. To the best of our knowledge the identifications of CCAP and NPF in T. urticae are the first for the Chelicerata. In addition, several novel orcokinins were identified from the scorpion Scorpiops jendeki and the spider Loxosceles laeta; in S. jendeki previously unknown isoforms of SIFamide, ESRNPPLNGSMFamide and ESKNPPLNGSMFamide, were also predicted. Taken collectively, the data presented in our study expand the catalog of known chelicerate neuropeptides and provide a foundation for future physiological studies of them in these animals.
