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Cloning and molecular characterization of tick kynurenine aminotransferase (HlKAT) from Haemaphysalis longicornis (Acari: Ixodidae).

Authors
  • Battsetseg, Badgar1
  • Boldbaatar, Damdinsuren
  • Battur, Banzragch
  • Xuan, Xuenan
  • Fujisaki, Kozo
  • 1 Laboratory of Emerging Infectious Diseases, Department of Frontier Veterinary Medicine, Kagoshima University, Korimoto 1-23-24, Kagoshima-shi, Kagoshima, 890-0065, Japan. , (Japan)
Type
Published Article
Journal
Parasitology Research
Publisher
Springer-Verlag
Publication Date
Sep 01, 2009
Volume
105
Issue
3
Pages
669–679
Identifiers
DOI: 10.1007/s00436-009-1439-4
PMID: 19381689
Source
Medline
License
Unknown

Abstract

A complementary DNA coding a novel kynurenine aminotransferase (KAT) molecule from Haemaphysalis longicornis tick embryo was cloned and characterized. The transcription of the HlKAT occurs at all stages during tick development as well as in the midgut, salivary glands, ovary, and synganglion of adult ticks, and protein expression levels increased during the blood-feeding course. The HlKAT gene without signal peptide was successfully expressed as a glutathione S-transferase fusion protein in soluble form, which is capable of catalyzing the transamination of kynurenine and 3-hydroxykynurenine to kynurenic acid and xanthurenic acid, respectively. The purified recombinant HlKAT showed dose-dependent inhibition effect on the growth of equine babesial parasite, Babesia caballi, in in vitro culture. All results suggested that a specific HlKAT is present in tick and HlKAT may play an important physiological role in H. longicornis. This is the first report of a member enzyme of tryptophan pathway in Chelicerata.

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