Schistosoma mansoni: Identification of SmNR4A, a member of nuclear receptor subfamily 4

Wenjie Wu, Philip T. LoVerde

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

A cDNA encoding a member of nuclear receptor subfamily 4 (SmNR4A) was isolated from the trematode Schistosoma mansoni. The open reading frame (ORF) of SmNR4A cDNA is 2481 base pairs long encoding an 827 amino acid protein. Alignment of the deduced protein sequence showed the DNA binding domain (DBD) of SmNR4A is highly conserved. Like human and Drosophila members in NR subfamily 4, SmNR4A possess an atypical ligand binding domain (LBD), the conserved lysine in helix H3 is replaced by a glutamic acid, and three of the four phenylalanines which fill the entire surface of the ligand binding pocket (LBP) are conserved in SmNR4A. A phylogenetic tree of SmNR4A was constructed using the conserved protein sequence of the DBD, the C-terminal-extension of DBD (CTE) and the LBD. The results show that the SmNR4A is a member of NR subfamily 4 from S. mansoni. The SmNR4A gene contains six exons spanning more than 50 kbp. The relative mRNA expression levels of SmNR4A were evaluated in 14 different developmental stages by quantitative real-time reverse-transcriptase polymerase chain reaction (q-PCR). The results demonstrated that SmNR4A expression was regulated throughout development. It was highly expressed in daughter sporocysts and 35-day worms, but barely expressed in cercariae and 1-h and 3-day schistosomules.

Original languageEnglish (US)
Pages (from-to)208-213
Number of pages6
JournalExperimental Parasitology
Volume120
Issue number2
DOIs
StatePublished - Oct 2008

Keywords

  • Gene organization
  • Nuclear receptor (NR)
  • Phylogenetic analysis
  • Platyhelminthes
  • Quantitative real-time reverse-transcriptase polymerase chain reaction (q-RT-PCR)
  • S. mansoni nuclear receptor NR4A
  • Schistosoma mansoni
  • SmNR4A
  • cDNA cloning

ASJC Scopus subject areas

  • Parasitology
  • Immunology
  • Infectious Diseases

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