Bacteriophage P22 Capsid as a Pluripotent Nanotechnology Tool

Viruses. 2023 Feb 13;15(2):516. doi: 10.3390/v15020516.

Abstract

The Salmonella enterica bacteriophage P22 is one of the most promising models for the development of virus-like particle (VLP) nanocages. It possesses an icosahedral T = 7 capsid, assembled by the combination of two structural proteins: the coat protein (gp5) and the scaffold protein (gp8). The P22 capsid has the remarkable capability of undergoing structural transition into three morphologies with differing diameters and wall-pore sizes. These varied morphologies can be explored for the design of nanoplatforms, such as for the development of cargo internalization strategies. The capsid proteic nature allows for the extensive modification of its structure, enabling the addition of non-native structures to alter the VLP properties or confer them to diverse ends. Various molecules were added to the P22 VLP through genetic, chemical, and other means to both the capsid and the scaffold protein, permitting the encapsulation or the presentation of cargo. This allows the particle to be exploited for numerous purposes-for example, as a nanocarrier, nanoreactor, and vaccine model, among other applications. Therefore, the present review intends to give an overview of the literature on this amazing particle.

Keywords: bacteriophage P22; nanoparticle; nanotechnology; protein cage; virus-like particles.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteriophage P22*
  • Capsid
  • Capsid Proteins / genetics
  • Cell Nucleus
  • Nanotechnology
  • Viroids*

Substances

  • Capsid Proteins

Grants and funding

VAMSAE received a master fellowship provided by Coordenação de aperfeiçoamento de Pessoal de Nıvel Superior (CAPES). JDSO and GHPN received a PhD fellowship provided by Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPQ). JRC had no research funding upon the production of this manuscript. Coordenação de aperfeiçoamento de Pessoal de Nível Superior (CAPES) Finance Code 001. This research received no external funding, and publication will be paid by J.R.C.’s personal funds.