ArticleMicrobial biotechnology2025
Development of a Recombinant Omicron BA.1 Subunit Vaccine Candidate in Pichia pastoris.
Article in Microbial biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- A Novel Chitin-Based Purification System Using GAL1 Fusion Tags: Enhancing Recombinant Protein Production While Retaining Biological Activity.Microbial biotechnology · 2025Article
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Authors and funding
18 authors.
Funding
Abstract
Low-cost and safe vaccines are needed to fill the vaccine inequity gap for future pandemics. Pichia pastoris is an ideal expression system for recombinant protein production due to its cost-effective and easy-to-scale-up process. Here, we developed a next-generation SARS-CoV2 Omicron BA.1-based recombinant vaccine candidate expressed in P. pastoris. The receptor binding domain of Omicron BA.1 spike protein (RBD-Omicron) was produced at 0.35 g/L in supernatant. With a 60% recovery after two-step purification, RBD-Omicron showed 99% purity. After in vitro characterisation of purified RBD-Omicron via chromatography, mass spectrometry, calorimetry and surface plasmon resonance-based methods, it was injected into mice for immunization studies. Three different doses of Alum and CpG adjuvanted RBD-Omicron were investigated and 10 μg RBD-Omicron gave the highest antigenicity. After two doses of vaccination, IgG titers in mice serum reached to more than 10
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