Characterization of squalene epoxidase encoding gene in dermatophyte pathogen Trichophyton violaceum

Subject Areas : Mycology

Fatemeh Noorbakhsh ¹ , Mehdi Mir Rahimi ² , Sasan Rezaei ³ , Hatef Ajodani far ⁴

1 - Assistant Professor, Department of Microbiology, Islamic Azad University, Varamin-Pishva Branch, Varamin, Iran.
2 - MS.c., Department of Microbiology, Islamic Azad University, Damghan Branch, Damghan, Iran.
3 - Professor, Department of Medical Mycology & Parasitology, Tehran University of Medical Sciences, Tehran, Iran.
4 - Assistant Professor, Department of Microbiology, Islamic Azad University, Damghan Branch, Damghan, Iran.

Received: 2012-11-30 Accepted : 2013-04-30 Published : 2013-10-01

Keywords: Dermatophyte, Trichophyton violaceum, Squalene epoxidase,

Abstract :

Background and Objectives: Trichophyton violaceum is one of the dermatophyte fungi which invades the skin, nail and hair of humans. Few studies were carried out in the field of molecular biology of this fungus. This study aimed to evaluate the presence of the squalene epoxidase encoding gene in Trichophyton violaceum. Materials and Methods: This sectional study was performed on the Trichophyton violaceum isolated from the patients who were visited at department of Mycology, Medical division of Tehran University. Following DNA extraction, the squalene epoxidase encoding gene was amplified by PCR preformed and its specified primers. The amplified gene was finally sequenced and its aminoacid sequences were identified. Results: Based on electrophoresis of PCR products, a fragment with 600bp nt was observed, which confirmed the amplification of squalene epoxidase gene. This gene was recorded in the national the NCBI gene bank as JX869101. This gene encodes a polypeptide with 220 aminoacids. PCR Nucleotide sequence comparison of this new gene with other existing genes in the gene bank revealed a significant homology with squalene epoxidase genes in other members of the fungi and other eukaryotes, as well. Conclusion: The aminoacid sequence of the encoded protein was about 78% identical to the sequence of squalene epoxidase from other fungi.