凡纳滨对虾血蓝蛋白与副溶血弧菌相互作用蛋白的鉴定海洋生物学专业论文.docxVIP

凡纳滨对虾血蓝蛋白与副溶血弧菌相互作用蛋白的鉴定海洋生物学专业论文.docx

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凡纳滨对虾血蓝蛋白与副溶血弧菌相互作用蛋白的鉴定海洋生物学专业论文

Abstract Shrimp aquaculture is one of the most important HYPERLINK /dict_result.aspx?searchword=%e6%b0%b4%e4%ba%a7%e5%85%bb%e6%ae%96%e4%b8%9aamp;tjType=sentenceamp;styleamp;t=aquaculture%2Bindustry aquaculture industry in our country. However, recently shrimp farms have suffered from dramatic decreases in production due to infectious diseases, mainly of bacterial and viral etiology. Researchers suggested that investigation of defense mechanisms and understanding of the interaction between host and the bacteria will be very helpful to establish ecological prevention strategies for shrimp disease control. Interestingly, recent reports reveal that hemocyanin in shrimp is a novel multifunctional protein with several immunological activities. Further studies showed that the potential interaction targets of bacterial binding to hemocyanin of bacterial might be the outer membrane proteins(Omps). But which Omps could interact to hemocyanin directly is still unclear. Thus, in this paper, an attempt was made to explore the interaction protein of Vibrio parahaemolyticus binding to hemocyanin from shrimp Litopenaeus vannamei, the main findings are as follows: An affinity incubation strategy was used to obtain Vibrio parahaemolyticus Omps binding to hemocyanin LH73(the hemocyanin purified by affinity chromatography using rabbit anti shrimp hemocyanin of 73kDa subunit antibody). SDSanalysis showed that there are four Omps which arranged from molecular weights of 35 to 45 kDa, which was named p1, p2, p3 and p4, respectively. MALDI-TOF-TOF analysis indicated that the p2 and p3 shared high homology with the OmpU and OmpC-like of Vibrio parahaemolyticus, respectively, suggesting that they might be the interacting proteins of Vibrio parahaemolyticus binding to hemocyanin. Based on the above results and our previous reports, the OmpU, OmpW and OmpC-like were further cloned. Sequence analysis indicated that the OmpW and OmpC-like were two novel sequences with the NCBI accession numbe

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