采用50 t电弧炉-50 t LF-60 t VD-180 mm×220 mm方坯连铸-热轧工艺生产F38MnVS非调质钢,在钢水入VD炉真空处理前加氮化锰线进行增氮操作,轧材后钢中氮含量稳定控制在(126-136)×10^(-6)钢材的力学性能、低倍组织、非金属夹杂...采用50 t电弧炉-50 t LF-60 t VD-180 mm×220 mm方坯连铸-热轧工艺生产F38MnVS非调质钢,在钢水入VD炉真空处理前加氮化锰线进行增氮操作,轧材后钢中氮含量稳定控制在(126-136)×10^(-6)钢材的力学性能、低倍组织、非金属夹杂物含量均满足用户要求。展开更多
目的:分析粉尘螨过敏原Der f 38的理化性质及结构特征,并综合生物信息学工具预测其免疫优势B、T细胞表位。方法:从世界卫生组织/国际免疫学联合会的过敏原数据库中获取Der f 38的氨基酸序列信息,利用ProtParam对Der f 38的理化性质特征...目的:分析粉尘螨过敏原Der f 38的理化性质及结构特征,并综合生物信息学工具预测其免疫优势B、T细胞表位。方法:从世界卫生组织/国际免疫学联合会的过敏原数据库中获取Der f 38的氨基酸序列信息,利用ProtParam对Der f 38的理化性质特征进行分析。通过SWISS-MODEL、AlphaFold2及GalaxyRefine对Der f 38的三维结构模型进行综合构建、优化得到最佳的蛋白模型。利用DNAStar Protean、Bepipred 2.0、ElliPro、DiscoTop、TepiTool进行Der f 38蛋白的B细胞线性、构象型表位以及T细胞表位的综合预测。结果:Der f 38为分子量13.99kDa且等电点为9.08,总平均亲水性为-0.337,不稳定指数为31.79。通过多种生物信息学工具综合分析,共得到4个优势B细胞线性表位、8个B细胞构象表位和8个T细胞表位。结论:Der f 38属于碱性蛋白,具有一定的亲水性和稳定性,含有多个免疫优势的B细胞和T细胞抗原表位,为进一步针对该蛋白的疫苗和过敏原特异性免疫疗法的设计与开发提供理论参考。展开更多
The envelope fusion protein F of baculoviruses is a class I viral fusion protein which play a significant role during virus entry into insect cells. F is initially synthesized as a precursor（F_0） and then cleaved in...The envelope fusion protein F of baculoviruses is a class I viral fusion protein which play a significant role during virus entry into insect cells. F is initially synthesized as a precursor（F_0） and then cleaved into a disulfide-linked F_1 and F_2 subunits during the process of protein maturation and secretion. To facilitate further investigation into the structure and function of F protein during virus infection, monoclonal antibodies（mAbs） against the F_2 subunit of Helicoverpa armigera nucleopolyhedrovirus（HearNPV）（Ha F） were generated. Two kinds of mAbs were obtained according to their different recognition epitopes： one kind of mAbs, as represented by 38F10,recognizes amino acid（aa） 85 to 123 of F_2 and the other kind, represented by 44D11, recognizes aa148 to 173 of F_2. Western blot and immunofluorescence assay confirmed that both of the mAbs recognized the F protein expressed in HearNPV infected cells, however, only 44D11 could neutralize HearNPV infection. The results further showed that 44D11 may not interact with a receptor binding epitope, rather it was demonstrated to inhibit syncytium formation in cells expressing the Ha F protein. The results imply that the monoclonal antibody 44D11 recognizes a region within HaF_2 that may be involved in the F-mediated membrane fusion process. 基金展开更多
文摘目的:分析粉尘螨过敏原Der f 38的理化性质及结构特征,并综合生物信息学工具预测其免疫优势B、T细胞表位。方法:从世界卫生组织/国际免疫学联合会的过敏原数据库中获取Der f 38的氨基酸序列信息,利用ProtParam对Der f 38的理化性质特征进行分析。通过SWISS-MODEL、AlphaFold2及GalaxyRefine对Der f 38的三维结构模型进行综合构建、优化得到最佳的蛋白模型。利用DNAStar Protean、Bepipred 2.0、ElliPro、DiscoTop、TepiTool进行Der f 38蛋白的B细胞线性、构象型表位以及T细胞表位的综合预测。结果:Der f 38为分子量13.99kDa且等电点为9.08,总平均亲水性为-0.337,不稳定指数为31.79。通过多种生物信息学工具综合分析,共得到4个优势B细胞线性表位、8个B细胞构象表位和8个T细胞表位。结论:Der f 38属于碱性蛋白,具有一定的亲水性和稳定性,含有多个免疫优势的B细胞和T细胞抗原表位,为进一步针对该蛋白的疫苗和过敏原特异性免疫疗法的设计与开发提供理论参考。
基金supported by the grants from the National Science Foundation of China (No. 31370191 and 31621061)the Strategic Priority Research Program of the Chinese Academy of Sciences (grant XDB11030400)Open Research Fund Program of the Key Laboratory of Agricultural and Environmental Microbiology, Chinese Academy of Sciences
文摘The envelope fusion protein F of baculoviruses is a class I viral fusion protein which play a significant role during virus entry into insect cells. F is initially synthesized as a precursor（F_0） and then cleaved into a disulfide-linked F_1 and F_2 subunits during the process of protein maturation and secretion. To facilitate further investigation into the structure and function of F protein during virus infection, monoclonal antibodies（mAbs） against the F_2 subunit of Helicoverpa armigera nucleopolyhedrovirus（HearNPV）（Ha F） were generated. Two kinds of mAbs were obtained according to their different recognition epitopes： one kind of mAbs, as represented by 38F10,recognizes amino acid（aa） 85 to 123 of F_2 and the other kind, represented by 44D11, recognizes aa148 to 173 of F_2. Western blot and immunofluorescence assay confirmed that both of the mAbs recognized the F protein expressed in HearNPV infected cells, however, only 44D11 could neutralize HearNPV infection. The results further showed that 44D11 may not interact with a receptor binding epitope, rather it was demonstrated to inhibit syncytium formation in cells expressing the Ha F protein. The results imply that the monoclonal antibody 44D11 recognizes a region within HaF_2 that may be involved in the F-mediated membrane fusion process. 基金
