Title Self-assembly of tail tube protein of bacteriophage vB_EcoS_NBD2 into extremely long polytubes in E. Coli and S. cerevisiae /
Authors Špakova, Aliona ; Šimoliūnas, Eugenijus ; Batiuškaitė, Raminta ; Pajeda, Simonas ; Meškys, Rolandas ; Petraitytė-Burneikienė, Rasa
DOI 10.3390/v11030208
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Is Part of Viruses.. Basel : MDPI AG. 2019, vol. 11, iss. 3, art. no. 208, p. [1-13].. ISSN 1999-4915
Keywords [eng] Bacteriophage vB_EcoS_NBD2 ; Escherichia coli ; Polytubes ; Saccharomyces cerevisiae ; Self-assembly ; Stability ; Tail tube protein ; Tubular structure
Abstract [eng] Nucleotides, peptides and proteins serve as a scaffold material for self-assembling nanostructures. In this study, the production of siphovirus vB_EcoS_NBD2 (NBD2) recombinant tail tube protein gp39 reached approximately 33% and 27% of the total cell protein level in Escherichia coli and Saccharomyces cerevisiae expression systems, respectively. A simple purification protocol allowed us to produce a recombinant gp39 protein with 85%–90% purity. The yield of gp39 was 2.9 ± 0.36 mg/g of wet E. coli cells and 0.85 ± 0.33 mg/g for S. cerevisiae cells. The recombinant gp39 self-assembled into well-ordered tubular structures (polytubes) in vivo in the absence of other phage proteins. The diameter of these structures was the same as the diameter of the tail of phage NBD2 (~12 nm). The length of these structures varied from 0.1 μm to >3.95 μm, which is 23-fold the normal NBD2 tail length. Stability analysis demonstrated that the polytubes could withstand various chemical and physical conditions. These polytubes show the potential to be used as a nanomaterial in various fields of science.
Published Basel : MDPI AG
Type Journal article
Language English
Publication date 2019