ArticleMicrobial cell factories2021
Molecular engineering improves antigen quality and enables integrated manufacturing of a trivalent subunit vaccine candidate for rotavirus.
Article in Microbial cell factories, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Swine Group A rotavirus vaccines: current status, adjuvant strategies, challenges, and future perspectives.Frontiers in veterinary science · 2026Review
- The Impact of Methanol Concentration on Recombinant Protein Glycosylation in Pichia pastoris SuperMan5.Microbial biotechnology · 2025Article
- Adaptation of Aglycosylated Monoclonal Antibodies for Improved Production in Komagataella phaffii.Biotechnology and bioengineering · 2025Article
- Biotechnological Interventions for the Production of Subunit Vaccines Against Group A Rotavirus.Cell biochemistry and function · 2024Review
- Recombinant bivalent subunit vaccine combining truncated VP4 from P[7] and P[23] induces protective immunity against prevalent porcine rotaviruses.Journal of virology · 2024Article
- Improving the secretion of designed protein assemblies through negative design of cryptic transmembrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Steric accessibility of the N-terminus improves the titer and quality of recombinant proteins secreted from Komagataella phaffii.Microbial cell factories · 2022Article
- Modular development enables rapid design of media for alternative hosts.Biotechnology and bioengineering · 2022Article
- Engineered SARS-CoV-2 receptor binding domain improves manufacturability in yeast and immunogenicity in mice.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Crystallization of a nonreplicating rotavirus vaccine candidate.Biotechnology and bioengineering · 2021Article
- Engineered SARS-CoV-2 receptor binding domain improves immunogenicity in mice and elicits protective immunity in hamsters.bioRxiv : the preprint server for biology · 2021Article
- Mechanism of Thimerosal-Induced Structural Destabilization of a Recombinant Rotavirus P[4] Protein Antigen Formulated as a Multi-Dose Vaccine.Journal of pharmaceutical sciences · 2021Article
- Rapid Developability Assessments to Formulate Recombinant Protein Antigens as Stable, Low-Cost, Multi-Dose Vaccine Candidates: Case-Study With Non-Replicating Rotavirus (NRRV) Vaccine Antigens.Journal of pharmaceutical sciences · 2021Article
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Authors and funding
19 authors.
Funding
Abstract
backgroundVaccines comprising recombinant subunit proteins are well-suited to low-cost and high-volume production for global use. The design of manufacturing processes to produce subunit vaccines depends, however, on the inherent biophysical traits presented by an individual antigen of interest. New candidate antigens typically require developing custom processes for each one and may require unique steps to ensure sufficient yields without product-related variants.
resultsWe describe a holistic approach for the molecular design of recombinant protein antigens-considering both their manufacturability and antigenicity-informed by bioinformatic analyses such as RNA-seq, ribosome profiling, and sequence-based prediction tools. We demonstrate this approach by engineering the product sequences of a trivalent non-replicating rotavirus vaccine (NRRV) candidate to improve titers and mitigate product variants caused by N-terminal truncation, hypermannosylation, and aggregation. The three engineered NRRV antigens retained their original antigenicity and immunogenicity, while their improved manufacturability enabled concomitant production and purification of all three serotypes in a single, end-to-end perfusion-based process using the biotechnical yeast Komagataella phaffii.
conclusionsThis study demonstrates that molecular engineering of subunit antigens using advanced genomic methods can facilitate their manufacturing in continuous production. Such capabilities have potential to lower the cost and volumetric requirements in manufacturing vaccines based on recombinant protein subunits.
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