Bakteriofagų struktūrinių baltymų panaudojimas savitvarkių nanostruktūrų surinkimui

The aim of this work was to expand current knowledge and explore a biotechnological potential of self-assembling nanostructures constructed from the structural proteins of newly identified bacteriophages. In this study, five new bacteriophages were characterized: Klebsiella sp. phage RaK2, Arthrobacter spp. phages ArV1 and ArV2, as well as Escherichia coli bacteriophages FV3 and NBD2. The structural proteins (in total 122) of these viruses were identified, of which 19 were selected for more detailed analysis. It was found that in vivo recombinant tail sheath proteins gp041 and gp053 from RaK2 and FV3, respectively, as well as the tail tube protein gp39 from NBD2, in the absence of other phage proteins, self-assemble into the ordered tubular structures. Optimization of purification procedures of gp053 was performed. It was determined that polysheaths formed by gp053 are extremely stable structures that are resistant to various environmental factors. To explore the polymerization properties of gp053, a set of gp053 mutants or gp053-based hybrid proteins was constructed. It was shown that the morphology of gp053-derived nanostructures depended both on the length and position of the insertion or deletion. The results presented here not only offer new insights into the diversity of bacterial viruses but they also provide the basis for the construction of hybrid nanostructures based on the structural proteins of bacteriophages