【摘 要】
：
In teleost,cathepsin B has been identified from several species and shown to play roles in the host immune response during pathogen challenge.However,the mechanism of how cathepsin B modulates the imm
【机 构】
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Key laboratory of Marine Biogenetics and Resources,Third Institute of Oceanography,State Oceanic Adm
【出 处】
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福建省海洋学会2014年学术年会暨福建省科协第十四届学术年会分会场
论文部分内容阅读
In teleost,cathepsin B has been identified from several species and shown to play roles in the host immune response during pathogen challenge.However,the mechanism of how cathepsin B modulates the immune response in teleosts remains poorly understood.In this study,we identified and characterized cathepsin B (LycCatB) and invariant chain (LycIi) from the large yellow croaker (Pseudosciaena crocea).Sequence comparison and phylogenetic analysis indicated that LycCatB and LycIi are highly conserved within teleosts.Quantitative RT-PCR analysis showed that LycCatB mRNA was widely expressed in all examined tissues.We then recombinantly expressed LycCatB and Lyc-TR-Ii (transmembrane domain removed Ii chain) in Pichia pastoris and E.coli,respectively.The recombinant LycCatB (rLycCatB) can hydrolyze the substrate Z-FR-AMC with a Km value of 40.68 μM.Furthermore,co-incubation of rLycCatB with rLyc-TR-Ii led to an efficient cleavage of rLyc-TR-Ii in a time-dependant manner.These results indicated that cathepsin B may be involved in MHC class II-associated Ii processing in large yellow croaker,and provide new information helping to elucidate the immunological functions of teleost cathepsin B.
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