vB_EcoS_NBD2 bacteriophage-originated polytubes as a carrier for the presentation of foreign sequences (original) (raw)

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.

Sign up for access to the world's latest research.

checkGet notified about relevant papers

checkSave papers to use in your research

checkJoin the discussion with peers

checkTrack your impact