Exploring the Landscape of the PP7 Virus-like Particle for Peptide Display.

ABSTRACT: Self-assembling virus-like particles (VLPs) can tolerate a wide degree of genetic and chemical manipulation to their capsid protein to display a foreign molecule polyvalently. We previously reported the successful incorporation of foreign peptide sequences in the junction loop and onto the C-terminus of PP7 dimer VLPs, as these regions are accessible for surface display on assembled capsids. Here, we report the implementation of a library-based approach to test the assembly tolerance of PP7 dimer capsid proteins to insertions or terminal extensions of randomized 15-mer peptide sequences. By performing two iterative rounds of assembly-based selection, we evaluated the degree of favorability of all 20 amino acids at each of the 15 randomized positions. Deep sequencing analysis revealed a dis

SUBMITTER: Keshavarz-Joud P 

PROVIDER: S-EPMC10540251 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature