Jpn. J. Infect. Dis., 58 (4), 214-217, 2005

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Original Article

Metalloprotease Gene of Arthroderma gypseum

Rui Kano*, Tsuyoshi Yamada1, Koichi Makimura1, Hideyo Yamaguchi1, Shinichi Watanabe2 and Atsuhiko Hasegawa

Department of Pathobiology, Nihon University School of Veterinary Medicine, Kanagawa 252-8510, 1Teikyo University, Institute of Medical Mycology and Genome Research Center, Teikyo University, Tokyo 192-0395 and 2Department of Dermatology, Teikyo University School of Medicine, Tokyo 173-8605, Japan

(Received February 7, 2005. Accepted April 6, 2005)

*Corresponding author: Mailing address: Department of Pathobiology, Nihon University School of Veterinary Medicine, 1866 Kameino, Fujisawa, Kanagawa 252-8510, Japan. Tel: +81-466-84-3649, Fax: +81-466-84-3649, E-mail: kano@brs.nihon-u.ac.jp


SUMMARY: The full-length cDNA sequence for metalloprotease (MEP) of Arthroderma gypseum (one of the teleomorphs of the Microsporum gypseum complex) was determined by the 5'-rapid amplification of cDNA ends (RACE) and 3'-RACE methods using cDNA as a template. The full-length cDNA sequence of the MEP (2,670 bp) gene was proved to encode 677 amino acids. The amino acid sequence of the A. gypseum MEP gene shared about 89 and 66% sequence similarity with the conserved region of the Microsporum canis MEP gene and Aspergillus fumigatus, respectively. Southern hybridization analysis of genomic DNA with an MEP probe gave many distinct bands in BamHI, EcoRI and HindIII digests of genomic DNA from A. gypseum. Reverse transcriptase-PCR analysis suggested that keratin might stimulate the expression of MEP mRNA in A. gypseum.

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