摘要
为了研究杆状病毒增强蛋白的活性基团 ,本文构建了分别表达三种N端部分缺失的粉纹夜蛾颗粒体病毒增强蛋白的重组杆状病毒 ,这三种蛋白在N端分别缺失了 15 0 ,186和 2 5 0个氨基酸。用重组病毒感染Tn 5B1 4细胞 ,成功地表达了这三种蛋白 ,并得到了纯化的蛋白质。通过体外降解围食膜的方法检测这些部分缺失的增强蛋白的活性 ,结果证实这三种蛋白均失去了增强蛋白的降解围食膜粘蛋白的活性。这一结果表明 。
Enhancin is a group of baculovirus proteins capable of increasing the infectivity of viruses in insect larvae, as well as the insecticidal effect of other biology control agents. In order to study the structure and function of enhancin from \%Trichoplusia ni granulovirus\%, recombinant baculoviruses were constrcuted to express truncated forms of enhancin with 150, 186 and 250 amino acids deleted from N terminal of native enhancin, respectively. The truncated enhancins were expressed successfully in Tn 5B1 4 cells. \%In vitro\% peritrophic membrane assay showed that all three truncated enhancin lost their mucin degrading ability, while a full length recombinant enhancin was active in the assay. It is concluded that the N terminal amino acids is essential for the mucin degrading activity of enhancin.
出处
《中国病毒学》
CSCD
2002年第4期326-330,共5页
Virologica Sinica
基金
国家自然科学基金会项目 (3 9870 0 0 6)