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. 2019 Jul 27;11(8):689. doi: 10.3390/v11080689

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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The ability of the purified recombinant Pr50^Gag-His₆-tag fusion protein to assemble in vitro to form virus-like particles (VLPs). (A–D) Transmission electron micrographs showing the morphology of the FIV Gag particles assembled in vitro in the presence of yeast tRNA. (B,D) Electron micrographs taken at higher magnifications are shown as insets. (E,F) Electron micrographs of negative control samples composed of an in vitro assembly buffer and purified protein in the absence of yeast tRNA. Scale bars represent 200 nm (43,000× magnification) for the wide field pictures and 50 nm (135,000× magnification) for the insets, respectively.