molecular characterization of cyclophilin protein gene in skin normal microflora: malassezia furfur

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.