Tehran University of Medical Sciences Iranian Journal of Public Health 2251-6085 38 2 2009 06 15 106 112 M Moazeni Division of Molecular Biology, Dept. of Medical Mycology & Parasitology, School of Public Health, Te F Noorbakhsh Islamic Azad University, Varamin-pishva Branch, Tehran, Iran F Zaini Division of Molecular Biology, Dept. of Medical Mycology & Parasitology, School of Public Health, Te P Kordbacheh Division of Molecular Biology, Dept. of Medical Mycology & Parasitology, School of Public Health, Te J Hashemi Division of Molecular Biology, Dept. of Medical Mycology & Parasitology, School of Public Health, Te B Mousavi Division of Molecular Biology, Dept. of Medical Mycology & Parasitology, School of Public Health, Te L Andonian S Rezaie Division of Molecular Biology, Dept. of Medical Mycology & Parasitology, School of Public Health, Te 2015 10 03 Background: Malassezia are dimorphic, lipid-dependent yeasts, which are responsible for causing several cutaneous and sys­temic conditions. Although cyclophilins (CyPs) are highly conserved cytosolic proteins that catalyze the peptidyl-prolyl cis-trans isomerazation reaction before protein folding process, it has been suggestive of an allergen in a few numbers of fungi such as Aspergillus fumigatus and Malassezia species. Allergenic cyclophilins are IgE-binding components, which have been characterized in other species of Malassezia; and are considered as Mala s 6 in Malassezia sympodialis.  In the pre­sent study we tried to identify the molecular characterization of cyclophilin gene in M. furfur. Methods: Pairs of oligonucleotide primers were designed from highly conserved regions of the gene counterparts in other fungi. The primers were then applied to amplify the primer-specific DNA fragment. Afterward, PCR product fragments were sequenced to be used in further analysis. Results: About 573 nucleotides, encoding a polypeptide of 190 amino acids, have been sequenced. Sequence comparison was performed in Gene Bank, both for the nucleotides and their deduced amino acid sequence. It revealed a significant homol­ogy with cyclophilin genes and proteins of other eukaryotic cells. The amino acid sequence of the encoded protein was about 86% identical to the sequence of cyclophilin protein from other fungi. Conclusion: The molecular characterization of cyclophilin gene may open the way to disclosure of the functional char­acteris­tics of cyclophilin and is a fundamental step for understanding the molecular basis of its pathogenesis in AEDS dis­ease. https://ijph.tums.ac.ir/index.php/ijph/article/view/3195 https://ijph.tums.ac.ir/index.php/ijph/article/download/3195/2994