PDF(Pubmed)
Abstract：
Non-infectious virus-like nanoparticles mimic native virus structures and can be modified by inserting foreign protein fragments, making them immunogenic tools for antigen presentation. This study investigated, for the first time, the immunogenicity of long and flexible polytubes formed by yeast-expressed tail tube protein gp39 of bacteriophage vB_EcoS_NBD2 and evaluated their ability to elicit an immune response against the inserted protein fragments. Protein gp39-based polytubes induced humoral immune response in mice, even without the use of adjuvant. Bioinformatics analysis guided the selection of protein fragments from Acinetobacter baumannii for insertion into the C-terminus of gp39. Chimeric polytubes, displaying 28-amino acid long OmpA protein fragment, induced IgG response against OmpA protein fragment in immunized mice. These polytubes demonstrated their effectiveness both as antigen carrier and an adjuvant, when the OmpA fragments were either displayed on chimeric polytubes or used alongside with the unmodified polytubes. Our findings expand the potential applications of long and flexible polytubes, contributing to the development of novel antigen carriers with improved immunogenicity and antigen presentation capabilities.
摘要：
非感染性病毒样纳米颗粒模拟天然病毒结构，可以通过插入外源蛋白片段进行修饰，使它们成为抗原呈递的免疫原性工具。这项研究调查了，第一次,由酵母表达的噬菌体vB_EcoS_NBD2的尾管蛋白gp39形成的长而柔性多管的免疫原性，并评估了它们引发针对插入的蛋白质片段的免疫应答的能力。基于蛋白gp39的多管诱导小鼠体液免疫应答，即使不使用佐剂。生物信息学分析指导从鲍曼不动杆菌中选择插入gp39C末端的蛋白质片段。嵌合聚管，显示28个氨基酸长的OmpA蛋白片段，在免疫小鼠中诱导针对OmpA蛋白片段的IgG应答。这些多管证明了它们作为抗原载体和佐剂的有效性，当OmpA片段显示在嵌合多管上或与未修饰的多管一起使用时。我们的发现扩展了长而柔性的聚管的潜在应用，有助于开发具有改进的免疫原性和抗原呈递能力的新型抗原载体。
