Cloning and characterization of Giardia intestinalis cyclophilin.
10.3347/kjp.2002.40.3.131
- Author:
Hak Sun YU
;
Hyun Hee KONG
;
Dong Il CHUNG
- Publication Type:Original article
- Keywords:
Giardia intestinalis;
cyclophilins;
cyclosporin;
peptidylprolyl isomerase
- MeSH:
Amino Acid Sequence;
Animals;
Cloning, Molecular;
Cyclophilins/antagonists & inhibitors/chemistry/genetics/*isolation&purification;
Cyclosporine/metabolism/pharmacology;
Giardia lamblia/*chemistry/genetics;
Human;
Immunosuppressive Agents;
Molecular Sequence Data;
Protein Binding;
Protozoan Proteins;
Recombinant Proteins
- From:The Korean Journal of Parasitology
2002;40(3):131-138
- CountryRepublic of Korea
- Language:English
-
Abstract:
The cyclophilins (Cyps) are family members of proteins that exhibit peptidylprolyl 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 (gicyp 1) was isolated. An open reading frame of gicyp 1 gene was 576 nucleotides, which corresponded to a translation product of 176 amino acids (Gicyp 1). 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 Gicyp 1, including tryptophan residue essential for the drug binding. The single copy of the gicyp 1 gene was detected in the G. intestinalis chromosome by southern hybridization analysis. Recombinant Gicyp 1 protein clearly accelerated the rate of cis--
