Schistosoma mansoni: SmE78, a nuclear receptor orthologue of Drosophila ecdysone-induced protein 78

Experimental Parasitology
Wenjie WuPhilip T LoVerde

Abstract

Drosophila ecdysone-induced protein 78 (E78) belongs to the nuclear receptor (NR) superfamily, it plays a role directly related to ecdysone signaling. We isolated a cDNA of Drosophila E78 orthologue from the Platyhelminth Schistosoma mansoni (SmE78). It is the first E78 orthologue known outside of the molting animals--the Ecdysozoa. The SmE78 cDNA is 3471 base pairs long and contains an entire open reading frame (ORF) encoding a 1087 amino acid protein. Phylogenetic analysis of the ligand-binding domain (LBD) demonstrates that the LBD of SmE78 is phylogenetically related to the Drosophila E78. Gene structure of SmE78 was determined showing it to consist of six exons spanning more than 32 kbp. Quantitative real-time reverse-transcriptase polymerase chain reaction (RT-PCR) demonstrated that SmE78 was expressed throughout schistosome development but with the highest levels of expression in miracidia and egg stage. The result is consistent with the previous studies that Ecdysterone was effective in stimulating host location activities in miracidia. The data suggest that SmE78 may be involved in transduction of an ecdysone signal in S. mansoni.

References

Jun 1, 1992·Computer Applications in the Biosciences : CABIOS·D T JonesJ M Thornton
Jun 1, 1991·In Vitro Cellular & Developmental Biology : Journal of the Tissue Culture Association·P O Lawrence
Sep 1, 1982·The Quarterly Review of Biology·M Bownes
Feb 1, 1996·Nature Structural Biology·J M WurtzH Gronemeyer
May 29, 2000·Parasitology Today·R L de MendonçaR J Pierce
Sep 21, 2000·Acta Tropica·L ChitsuloL Savioli
Aug 29, 2001·Bioinformatics·J P Huelsenbeck, F Ronquist
Dec 1, 2001·Annual Review of Entomology·James W Truman, Lynn M Riddiford
Jan 30, 2002·Molecular and Biochemical Parasitology·Kirsten CrossgroveClaude V Maina
Feb 16, 2002·Methods : a Companion to Methods in Enzymology·K J Livak, T D Schmittgen
Oct 17, 2002·Trends in Parasitology·Nils Robert Bergquist
Nov 9, 2002·European Journal of Biochemistry·Ricardo L De MendonçaRaymond J Pierce
Jul 2, 2004·Molecular Biology and Evolution·Stéphanie BertrandMarc Robinson-Rechavi
Apr 11, 2006·Molecular and Biochemical Parasitology·Rong HuPhilip T Loverde
Jul 15, 2006·International Journal for Parasitology·Rong HuPhilip T LoVerde
Jul 28, 2006·Molecular and Biochemical Parasitology·Changxue LuPhilip T LoVerde

❮ Previous
Next ❯

Citations

Jul 28, 2009·Annual Review of Genomics and Human Genetics·Ze-Guang HanZhu Chen
Nov 11, 2009·PLoS Neglected Tropical Diseases·Marcela G DrummondGlória R Franco
Dec 12, 2012·Journal of Molecular Graphics & Modelling·Mainá BitarGlória Regina Franco
Aug 7, 2008·Experimental Parasitology·Wenjie Wu, Philip T Loverde
Dec 30, 2015·PLoS Neglected Tropical Diseases·Peter D ZinielDavid L Williams
May 16, 2013·Parasitology·Elizângela A RochaGlória R Franco
Jan 1, 2016·PLoS Neglected Tropical Diseases·Letícia AndersonSergio Verjovski-Almeida
Feb 7, 2017·The Journal of Clinical Investigation·Zhu WangDavid J Mangelsdorf

❮ Previous
Next ❯

Related Concepts

Related Feeds

Anthelmintics

Anthelmintics or antihelminthics are a group of antiparasitic drugs that expel parasitic worms (helminths) and other internal parasites from the body by either stunning or killing them and without causing significant damage to the host. Discover the latest research on anthelmintics here.

Anthelmintics (ASM)

Anthelmintics or antihelminthics are a group of antiparasitic drugs that expel parasitic worms (helminths) and other internal parasites from the body by either stunning or killing them and without causing significant damage to the host. Discover the latest research on anthelmintics here.