Leucine Aminopeptidase in the Ixodid Tick Haemaphysalis longicornis: Endogenous Expression Profiles in Midgut

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  • HATTA Takeshi
    Laboratory of Parasitic Diseases, National Institute of Animal Health, National Agricultural and Food Research Organization
  • TSUJI Naotoshi
    Laboratory of Parasitic Diseases, National Institute of Animal Health, National Agricultural and Food Research Organization
  • MIYOSHI Takeharu
    Laboratory of Parasitic Diseases, National Institute of Animal Health, National Agricultural and Food Research Organization
  • ALIM M. Abdul
    Laboratory of Parasitic Diseases, National Institute of Animal Health, National Agricultural and Food Research Organization
  • ISLAM M. Khyrul
    Laboratory of Parasitic Diseases, National Institute of Animal Health, National Agricultural and Food Research Organization
  • FUJISAKI Kozo
    National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine Laboratory of Emerging Infectious Diseases, School of Frontier Veterinary Medicine, Kagoshima University

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  • Parasitology: Leucine aminopeptidase in the ixodid tick Haemaphysalis longicornis: endogenous expression profiles in midgut

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Abstract

We previously identified a cDNA from the ixodid tick Haemaphysalis longicornis that encodes leucine aminopeptidase, HlLAP. Functionally, recombinant HlLAP effectively hydrolyzed synthetic amino acid derivatives. Here, we investigated the temporal expression profiles of midgut HlLAP in adult H. longicornis parthenogenetic ticks from the starting of blood feeding until just before the onset of oviposition. Midgut HlLAP transcript expression level was higher during post-engorgement period than that during feeding period. Endogenous HlLAP in the midgut was also observed with higher expression level during post-engorgement period. Histological localization of HlLAP was in the cytosol of midgut epithelial cells, notably the newly differentiated basophilic cells at post-engorgement. Our data suggested that HlLAP was dominantly localized in basophilic cells, where it may play regulatory roles in protein biosynthesis and degradation.<br>

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