Molecular Characterization of Cyclophilin Protein Gene in Skin Normal Microflora: Malassezia furfur

Malassezia are dimorphic, lipid-dependent yeasts, which are responsible for causing several cutaneous andsystemic conditions. although cyclophilins (cyps) are highly conserved cytosolic proteins that catalyze the peptidyl-prolylcis-trans isomerazation reaction before protein folding process, it has been suggestive of an allergen in a few numbers offungi such as aspergillus fumigatus and malassezia species. allergenic cyclophilins are ige-binding components, whichhave been characterized in other species of malassezia; and are considered as mala s 6 in malassezia sympodialis. in thepresent 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 otherfungi. the primers were then applied to amplify the primer-specific dna fragment. afterward, pcr product fragments weresequenced to be used in further analysis.results: about 573 nucleotides, encoding a polypeptide of 190 amino acids, have been sequenced. sequence comparisonwas performed in gene bank, both for the nucleotides and their deduced amino acid sequence. it revealed a significanthomology with cyclophilin genes and proteins of other eukaryotic cells. the amino acid sequence of the encoded proteinwas 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 characteristicsof cyclophilin and is a fundamental step for understanding the molecular basis of its pathogenesis in aeds disease.