The mature Head II form of the HK97 virus-like particle (VLP) derived from the bacteriophage HK97 has been identified as a unique nanoplatform for use in the construction of bionanomaterials. The Head II VLP is a highly stable nanoparticle with a diameter of 60 nm and has unique stability properties resulting from the crosslinking of the coat protein GP5 subunits to form a catenane structure (analogous to molecular chain mail). For the formation of the Head II VLP, the HK97 coat protein (GP5) is co-expressed with a maturation protein, GP4, that becomes encapsulated inside the precursor Prohead HK97 VLP. GP4 proteolytically cleaves GP5, which allows eventual maturation to the Head II form. While investigating a co-expression strategy of GP5 and GP4 for producing the Head II HK97 VLP, a mutation of an amino acid in GP5 was found to improve the stability of Prohead HK97 VLPs and the overall production yield and formation of the Head II HK97 VLP. The results presented here are for examining GP5 mutants for obtaining improved yields and stable formation of the Head II HK97 VLP using a recombinant co-expression strategy in <i>E. coli</i>.

Optimizing the production yield and stability of the HK97 head II virus like particle produced from <i>Escherichia coli</i>

ACS Spring 2022

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Optimizing the production yield and stability of the HK97 head II virus like particle produced from Escherichia coli