Eimeria tenella: genomic organization and expression of an 89kDa cyclophilin

Though parasite cyclophilins are promising new drug targets, Eimeria tenella cyclophilins have not been characterized yet. Here, we describe an 89kDa cyclophilin, designated EtCYP89. It is expressed throughout the developmental cycle of E. tenella, both in the intracellular stages in chicken and in...

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Bibliographic Details
Published in:Experimental parasitology 2008-02, Vol.118 (2), p.275-279
Main Authors: Hosse, Ralf J, Krücken, Jürgen, Bierbaum, Stefan, Greif, Gisela, Wunderlich, Frank
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Chickens
Cyclophilins - biosynthesis
Cyclophilins - chemistry
Cyclophilins - genetics
DNA, Complementary - chemistry
Eimeria tenella
Eimeria tenella - genetics
Eimeria tenella - growth & development
Eimeria tenella - metabolism
Gene Expression
Genome, Protozoan - physiology
Male
Molecular Sequence Data
Open Reading Frames
Phylogeny
Reverse Transcriptase Polymerase Chain Reaction
RNA, Protozoan - genetics
Sequence Alignment
Toxoplasma gondii
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Summary:Though parasite cyclophilins are promising new drug targets, Eimeria tenella cyclophilins have not been characterized yet. Here, we describe an 89kDa cyclophilin, designated EtCYP89. It is expressed throughout the developmental cycle of E. tenella, both in the intracellular stages in chicken and in extracellular sporulated oocysts and sporozoites. The EtCYP89 protein contains two Ser-rich domains in its NH2-terminus separated by a His-rich stretch. WD40 repeats are localized in the central part of the protein followed by a cyclophilin domain at the COOH-terminus. Both protein and genomic organization of EtCyp89 are conserved in comparison with its ortholog TgCyp81.6 in Toxoplasma gondii, except for the absence of a Ser- and His-rich NH2-terminus in TgCYP81.6. In particular, those 13 residues are conserved which are responsible for binding the anti-coccidial drug cyclosporine A.
ISSN:0014-4894
DOI:10.1016/j.exppara.2007.07.013