Parasites, Hosts and Diseases

"peptidylprolyl isomerase"

Original Article

Cloning and characterization of Giardia intestinalis cyclophilin: Hak-Sun Yu, Hyun-Hee Kong, Dong-Il Chung; Korean J Parasitol 2002;40(3):131-138.
Published online September 30, 2002; DOI: https://doi.org/10.3347/kjp.2002.40.3.131

Abstract
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The cyclophilins (Cyps) are family members of proteins that exhibit peptidyl-prolyl cis-trans isomerase (PPIase, EC 5.2.1.8) activity and bind the immunosuppressive agent cyclosprin A (CsA) in varying degrees. During the process of random sequencing of a cDNA library made from Giardia intestinalis WB strain, the cyclophilin gene (gicyp1) was isolated. An open reading frame of gicyp1 gene was 576 nucleotides, which corresponded to a translation product of 176 amino acids (Gicyp1). The identity with other Cyps was about 58-71%. The 13 residues that constituted the CsA binding site of human cyclophilin were also detected in the amino acid sequence of Gicyp1, including tryptophan residue essential for the drug binding. The single copy of the gicyp1 gene was detected in the G. intestinalis chromosome by southern hybridization analysis. Recombinant Gicyp1 protein clearly accelerated the rate of cis → trans isomerization of the peptide substrate and the catalysis was completely inhibited by the addition of 0.5 ?M CsA.

Citations

Citations to this article as recorded by

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Parasites & Vectors.2025;[Epub] CrossRef
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International Journal for Parasitology.2006; 36(3): 261. CrossRef
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