Order Caudovirales
Paul Pumpens, Peter Pushko, Philippe Le Mercier in Virus-Like Particles, 2022
The phage P22, a member of the Salmonella virus P22 species, infects Salmonella typhimurium when intact tail fibers are present. The early experiments (Prevelige et al. 1988) demonstrated that the coat and scaffolding subunits derived from the procapsids of the phage P22 coassembled rapidly and efficiently into icosahedral shells in vitro under native conditions, and the in vitro reaction exhibited the regulated features observed in vivo, while neither coat nor scaffolding subunits alone self-assembled into large structures. Upon simply mixing the subunits together, they polymerized into procapsid-like shells with the in vivo coat and scaffolding protein composition. The subunits in the purified coat protein preparations are monomeric. These results confirmed that the P22 procapsid formation did not proceed through the assembly of a core of scaffolding, which then organized the coat but required copolymerization of coat and scaffolding (Prevelige et al. 1988). Furthermore, due to the long-standing efforts of the famous Trevor Douglas team by the highly advanced P22-based protein cargo tools, this phage became a definite grand of the viral nanotechnology. Thanks to their ingenious solutions, the P22 VLPs paved a way for further multidisciplinary applications.
Mechanisms of cellular and humoral immunity through the lens of VLP-based vaccines
Published in Expert Review of Vaccines, 2022
Hunter McFall-Boegeman, Xuefei Huang
Similar to Qß, most VLPs are aided in assembly by interactions between RNA and proteins, usually via a hairpin loop in the RNA with the interior of the CP[18,42]. A small minority, typically double stranded DNA (dsDNA) viruses, utilize interactions between a scaffold protein and the CP. One of the most common examples is the enterobacteria phage P22. The recombinantly expressed VLP is a T = 7 icosahedron made up of 420 copies of the CP and ~250 copies of the scaffolding protein[43]. The scaffold protein is amenable to a large range of modifications allowing for easy loading of the capsid interior[44].
Related Knowledge Centers
- Bacteriophage
- Molecular Biology
- Mutation
- Operon
- Podoviridae
- Protein
- Transduction
- Salmonella Enterica Subsp. Enterica
- Gene
- Lambda Phage