Virus-based nanoparticles constitute a promising platform for the creation of efficient vaccines and nanomaterials. Previously we demonstrated, that the recombinant tail tube protein gp39 of vB_EcoS_NBD2 bacteriophage self-assembles into extremely long (from 0.1 to >3.95 μm), flexible, and stable polytubes when produced in Saccharomyces cerevisiae. To develop a tubular platform for multivalent display of foreign antigens, yeast-derived recombinant tail tube protein gp39 was chosen as a scaffold. The carboxy-terminal fusions of gp39 with various antigens up to 238 amino acids in length resulted in different synthesis efficiency and self-assembly capacity. Recombinant gp39 fused with green fluorescent protein (eGFP) comprising 238 amino acid residues was capable to self-assemble into short fluorescent polytubes with retained eGFP functional activity. By demonstrating the display of active foreign antigens on the exterior surface of polytubes, these structures may provide a promising tool for diverse applications in nanotechnology.

基于病毒的纳米粒子构成了一个有前途的平台，用于创建有效的疫苗和纳米材料。之前我们证明，当在酿酒酵母中生产时，vB_EcoS_NBD2 噬菌体的重组尾管蛋白 gp39 自组装成极长（从 0.1 到 >3.95 μm）、灵活且稳定的多管. 为了开发用于外源抗原多价展示的管状平台，选择酵母衍生的重组尾管蛋白 gp39 作为支架。gp39 与各种抗原的羧基末端融合长达 238 个氨基酸，导致不同的合成效率和自组装能力。与包含 238 个氨基酸残基的绿色荧光蛋白 (eGFP) 融合的重组 gp39 能够自组装成具有保留 eGFP 功能活性的短荧光多管。通过在多管的外表面上展示活性外来抗原，这些结构可能为纳米技术的各种应用提供有前途的工具。