TY - JOUR
T1 - Molecular characterization and comparative study of 6 salivary gland metalloproteases from the hard tick, Haemaphysalis longicornis
AU - Harnnoi, Thasaneeya
AU - Sakaguchi, Takeshi
AU - Nishikawa, Yoshifumi
AU - Xuan, Xuenan
AU - Fujisaki, Kozo
N1 - Funding Information:
This work was supported by grants from the Bio-orientated Technology Research Advancement Institution (BRAIN), the 21st Century COE program (A-1) from the Ministry of Education, Science, Sports, and Culture of Japan, and Grants-in-Aid for Scientific Research from the Japan Society for the Promotion of Sciences.
PY - 2007/5/1
Y1 - 2007/5/1
N2 - Six genes encoding metalloproteases were identified from the salivary gland of the hard tick, Haemaphysalis longicornis. Comparative analyses have shown the evolutionary distinct and different mRNA expression patterns of each gene during blood feeding. The proteins are synthesized as proenzymes with a prodomain and a metalloprotease/cysteine-rich domain of the reprolysin family. Within the active site, amino acid substitutions were observed. The recombinant Escherichia coli expression of one gene, hlESTMP1, was performed. The immunoblot analysis and indirect fluorescent assay using anti-hlESTMP1 suggested that this protein is mainly expressed in the cytoplasm of the salivary glands and only the mature form of 34 kDa was detectable. The proenzyme expressed by baculovirus was processed into a mature domain, suggesting that proenzyme activation possibly occurs through a pro-protein convertase dependent pathway. The presence of these diverse enzymes might contribute to the greater functional complexity of bioactive molecules in tick saliva to facilitate blood feeding.
AB - Six genes encoding metalloproteases were identified from the salivary gland of the hard tick, Haemaphysalis longicornis. Comparative analyses have shown the evolutionary distinct and different mRNA expression patterns of each gene during blood feeding. The proteins are synthesized as proenzymes with a prodomain and a metalloprotease/cysteine-rich domain of the reprolysin family. Within the active site, amino acid substitutions were observed. The recombinant Escherichia coli expression of one gene, hlESTMP1, was performed. The immunoblot analysis and indirect fluorescent assay using anti-hlESTMP1 suggested that this protein is mainly expressed in the cytoplasm of the salivary glands and only the mature form of 34 kDa was detectable. The proenzyme expressed by baculovirus was processed into a mature domain, suggesting that proenzyme activation possibly occurs through a pro-protein convertase dependent pathway. The presence of these diverse enzymes might contribute to the greater functional complexity of bioactive molecules in tick saliva to facilitate blood feeding.
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U2 - 10.1016/j.cbpb.2006.12.008
DO - 10.1016/j.cbpb.2006.12.008
M3 - Article
C2 - 17292650
AN - SCOPUS:33947572495
VL - 147
SP - 93
EP - 101
JO - Comparative biochemistry and physiology. B, Comparative biochemistry
JF - Comparative biochemistry and physiology. B, Comparative biochemistry
SN - 1096-4959
IS - 1
ER -