Hlcyst-1 and Hlcyst-2 are Potential Inhibitors of HlCPL-A in the Midgut of the Ixodid Tick Haemaphysalis longicornis

  • YAMAJI Kayoko
    Graduate School of Life and Environmental Sciences, University of Tsukuba National Institute of Animal Health, National Agriculture and Food Research Organization National Institute of Livestock and Grassland Science, National Agriculture and Food Research Organization
  • TSUJI Naotoshi
    National Institute of Animal Health, National Agriculture and Food Research Organization Graduate School of Agricultural and Life Sciences, The University of Tokyo
  • MIYOSHI Takeharu
    National Institute of Animal Health, National Agriculture and Food Research Organization
  • HATTA Takeshi
    National Institute of Animal Health, National Agriculture and Food Research Organization
  • ALIM M. Abdul
    National Institute of Animal Health, National Agriculture and Food Research Organization
  • ANISUZZAMAN
    National Institute of Animal Health, National Agriculture and Food Research Organization Graduate School of Agricultural and Life Sciences, The University of Tokyo
  • KUSHIBIKI Shiro
    Graduate School of Life and Environmental Sciences, University of Tsukuba National Institute of Livestock and Grassland Science, National Agriculture and Food Research Organization
  • FUJISAKI Kozo
    Department of Frontier Veterinary Medicine, Kagoshima University

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Other Title
  • Parasitology: Hlcyst-1 and Hlcyst-2 are potential inhibitors of HlCPL-A in the midgut of the ixodid tick Haemaphysalis longicornis

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Abstract

Although the actions of cysteine proteases are controlled in part by endogenous tight-binding cysteine protease inhibitors from the cystatin superfamily, regulatory mechanisms used by ticks to control protease activities are unknown. We report here the interaction of 2 endogenous midgut cysteine protease inhibitors, Hlcyst-1 and Hlcyst-2, with an endogenous midgut cysteine protease, HlCPL-A in Haemaphysalis longicornis. In vitro inhibition assays demonstrated that the hydrolytic activity of HlCPL-A was inhibited by Hlcyst-1 and Hlcyst-2 in dose dependent manner. Immunofluorescent studies revealed that Hlcyst-1 and Hlcyst-2 are co-localized with HlCPL-A in the epithelial cells of the midgut. The hemoglobin degradation activity of HlCPL-A was dose-dependently inhibited by Hlcyst-1 and Hlcyst-2. These results strongly indicate that, Hlcyst-1 and Hlcyst-2 are possible inhibitor of HlCPL-A and play a key role in regulatory mechanisms of hemoglobin degradation process in ticks.<br>

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