| Comparison of enzymatic activities between the recombinant CHT1 proteins from the hard tick Haemaphysalis longicornis expressed in E. coli and baculovirus-mediated Sf 9 cells |
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Myung-Jo You, Kozo Fujisaki |
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National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine |
| E. coli와 baculovirus-mediated Sf 9 세포에서 발현된 진드기 H. longicornis의 CHT1 단백의 효소활성 비교 |
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유명조, 고조후지사끼 |
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오비히로축산대학 국립원충성질병연구센터 |
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| Abstract |
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A chitinase cDNA named CHT1 was cloned from the hard tick, Haemaphysalis longicornis, and the enzymatic properties of its recombinant proteins were characterized. The CHT1 cDNA encodes 930 amino-acid (aa) residues including a 22 aa putative signal peptide, with the calculated molecular mass of the putative mature protein 104 kDa. The E coli-expressed rCHT1 exhibited weak chitinolytic activity against $4MU-(GlcNAc)_3$. The rCHT1 protein with higher activity was obtained using recombinant Autographa californica multiple nuclear polyhedrosis virus (AcMNPV), which expresses rCHT1 under polyhedrin promoter. These findings suggest that the rCHT1 expressed in baculovirus-mediated Sf 9 cells has a high activity than E coli-expressed rCHT1. |
| Key Words:
tick, Haemaphysalis longicornis, chitinase, recombinant protein |
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