Abstract
The serine proteases with clip domain are involved in various innate immune functions in invertebrate such as antimicrobial activity, cell adhesion, pattern recognition and regulation of the prophenoloxidase system. A serine protease with clip-domain cDNA (Cf SP) was obtained by Expressed sequence taggings (ESTs) method and rapid amplification of cDNA ends (RACE). The Cf SP full-length cDNA was of 1,152 bp, including a 5′-terminal untranslated region (UTR) of 63 bp, a 3′-terminal UTR of 81 bp with a canonical polyadenylation signal sequence AATAAA and a poly(A) tail, and an open reading frame of 1,008 bp encoding a polypeptide of 336 amino acids with a putative signal peptide of 19 amino acids. The deduced amino acid sequence of Cf SP contained an amino-terminal clip domain with three disulfide bonds formed six conserved Cys residues, a carboxyl-terminal trypsin-like domain with the conserved His–Asp–Ser catalytic triad, and a low complexity linker sequence. The Cf SP was strongly expressed in hemocytes and the mRNA expression of Cf SP was up-regulated and increased 3.2-fold and 2.6-fold at 16 h after injection of Vibrio anguillarum and Micrococcus luteus. The results suggested that Cf SP gene might be involved in immune response of Gram-negative and Gram-positive microbial infection in scallop
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Acknowledgements
The authors would like to thank all laboratory members for technical advice and helpful discussions. This research was supported by 863 High Technology Project (No. 2002AA626020) from the Chinese Ministry of Science and Technology, the grant (No. 40276045 and 30230280) from NSFC to Dr. Linsheng Song and Prof. Jianhai Xiang, and the grant (No.06SB011014) from South China Sea Institute of Oceanography, Chinese Academy of Sciences to Dr. Ling Zhu.
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Zhu, L., Song, L., Mao, Y. et al. A novel serine protease with clip domain from scallop Chlamys farreri . Mol Biol Rep 35, 257–264 (2008). https://doi.org/10.1007/s11033-007-9078-2
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DOI: https://doi.org/10.1007/s11033-007-9078-2