A thrombin inhibitor from the ixodid tick, Amblyomma hebraeum |
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Authors: | Lai Ren Takeuchi Hajime Jonczy Jan Rees Huw H Turner Philip C |
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Affiliation: | Cell Regulation and Signalling Division, School of Biological Sciences, University of Liverpool, Biosciences Building, Crown Street, Liverpool L69 7ZB, UK. |
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Abstract: | A novel thrombin inhibitor named Amblin was identified from the haemolymph of the ixodid (hard) tick, Amblyomma hebraeum, and the coding cDNA was isolated from a tick cDNA library. This cDNA codes for a preprotein of 166 amino acids, including a predicted signal peptide composed of 15 amino acids N-terminal to the mature Amblin. The 151-amino-acid mature Amblin contains 14 cysteines and two Kunitz-like domains. It displays high sequence similarity with a tissue factor pathway inhibitor (TFPI), Ixolaris, from the ixodid tick, Ixodes scapularis, which has 10 cysteines, and a thrombin inhibitor, Boophilin, from the ixodid tick, Boophilus microplus, which has 12 cysteines. Recombinant Amblin specifically inhibited thrombin as efficiently as native Amblin did. This is the first report of a thrombin inhibitor from tick haemolymph. |
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