ArticleJournal of pharmaceutical sciences2020
Characterizing and Minimizing Aggregation and Particle Formation of Three Recombinant Fusion-Protein Bulk Antigens for Use in a Candidate Trivalent Rotavirus Vaccine.
Article in Journal of pharmaceutical sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Real-Time Single-Aggregate Analysis of Vaccine Antigen Stability via Stochastic Electrochemical Blocking.The AAPS journal · 2026Article
- Thermostability of tetanus toxoid vaccine encapsulated in metal-organic frameworks.Drug delivery and translational research · 2025Article
- The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure.Science advances · 2024Article
- Immunoinformatics-guided approach for designing a pan-proteome multi-epitope subunit vaccine against African swine fever virus.Scientific reports · 2024Article
- Concordance of in vitro and in vivo measures of non-replicating rotavirus vaccine potency.Vaccine · 2022Article
- Crystallization of a nonreplicating rotavirus vaccine candidate.Biotechnology and bioengineering · 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
- Formulation and preclinical studies with a trivalent rotavirus P2-VP8 subunit vaccine.Human vaccines & immunotherapeutics · 2020Article
- Recombinant Subunit Rotavirus Trivalent Vaccine Candidate: Physicochemical Comparisons and Stability Evaluations of Three Protein Antigens.Journal of pharmaceutical sciences · 2020Article
- Effect of Aluminum Adjuvant and Preservatives on Structural Integrity and Physicochemical Stability Profiles of Three Recombinant Subunit Rotavirus Vaccine Antigens.Journal of pharmaceutical sciences · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In a companion paper, the structural integrity, conformational stability, and degradation mechanisms of 3 recombinant fusion-protein antigens comprising a non-replicating rotavirus (NRRV) vaccine candidate (currently being evaluated in early-stage clinical trials) are described. In this work, we focus on the aggregation propensity of the 3 NRRV antigens coupled to formulation development studies to identify common frozen bulk candidate formulations. The P2-VP8-P[8] antigen was most susceptible to shaking and freeze-thaw-induced aggregation and particle formation. Each NRRV antigen formed aggregates with structurally altered protein (with exposed apolar regions and intermolecular β-sheet) and dimers containing a non-native disulfide bond. From excipient screening studies with P2-VP8-P[8], sugars or polyols (e.g., sucrose, trehalose, mannitol, sorbitol) and various detergents (e.g., Pluronic F-68, polysorbate 20 and 80, PEG-3350) were identified as stabilizers against aggregation. By combining promising additives, candidate bulk formulations were optimized to not only minimize agitation-induced aggregation, but also particle formation due to freeze-thaw stress of P2-VP8-P[8] antigen. Owing to limited material availability, stabilization of the P2-VP8-P[4] and P2-VP8-P[6] was confirmed with the lead candidate P2-VP8-P[8] formulations. The optimization of these bulk NRRV candidate formulations is discussed in the context of subsequent drug product formulations in the presence of aluminum adjuvants.
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