School of Chemical Engineering and Technology, Tianjin University, Tianjin 300350, China
This work was supported by grants from The National Natural Science Foundation of China (91534119, 21621004) and the Innovation Foundation of Tianjin University.
The virus-like particle (VLP) of murine polyomavirus (MPV) is a spherical shell with nanostructure. It assembles from protein VP1, the major structural protein of capsid. MPV VLP has a unique nanostructure that can self-assemble in vivo or in vitro and many sites that can be modified. The special architecture make it an ideal nanoscale model in scientific fields such as biochemistry. With the modification of the protein capsid and the transformation of the core cavity, researchers have developed a series of vaccines, multifunctional diagnostic agents and versatile nanocage systems. Recent studies of MPV VLP modification have focused on the interface modification between subunits to facilitate the assemble process, and the interior or exterior modification to develop diverse applications. This paper reviews the structural characteristics of MPV VLP, and briefly introduces the expression systems and assembly mechanism. The modification of MPV VLP was summarized, with emphasis on chemical modification and modification using genetic engineering. In addition, the applications of MPV VLP in the fields of vaccine development, delivery of drug and other molecules were described with examples. Then the prospect of research on MPV VLP was discussed, focusing on the large-scale production and in-depth analysis of assembly mechanism, beneficial from the use of advanced science and technology.
LI Guo-An, ZHANG Lin. Research Progress of Murine Polyomavirus Virus-like Particle and Its Application in Vaccine Development[J]. Progress in Biochemistry and Biophysics,2019,46(8):760-771
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