Optimization, characterization, comparison of self-assembly VLP of capsid protein L1 in yeast and reverse vaccinology design against human papillomavirus type 52

BackgroundVaccination is the one of the agendas of many countries to reduce cervical cancer caused by the Human papillomavirus. Currently, VLP-based vaccine is the most potent vaccine against HPV, which could be produced by a variety of expression systems. Our study focuses on a comparison of recombinant protein expression L1 HPV52 using two common yeasts, Pichia pastoris and Hansenulapolymorpha that have been used for vaccine production on an industrial scale. We also applied bioinformatics approach using reverse vaccinology to design alternative multi-epitope vaccines in recombinant protein and mRNA types.ResultsOur study found that P.pastoris relatively provided higher level of L1 protein expression and production efficiency compared to H.polymorpha in a batch system. However, both hosts showed self-assembly VLP formation and stable integration during protein induction. The vaccine we have designed exhibited high immune activation and safe in computational prediction. It is also potentially suitable for production in a variety of expression systems.ConclusionBy monitoring the overall optimization parameter assessment, this study can be used as the basis reference for large-scale production of the HPV52 vaccine.

Automated summary

This study compares the ability of two common yeasts, Pichia pastoris and Hansenulapolymorpha, to express L1 HPV52 recombinant protein for industrial-scale production. It is found that P.pastoris provides relatively higher levels of L1 protein expression and production efficiency compared to H.polymorpha in a batch system. The vaccine designed in this study exhibits high immune activation and safety in computational prediction and is potentially suitable for production in a variety of expression systems.