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A rapid and simple screening method to identify conditions for enhanced stability of modular vaccine candidates

Paper ID Volume ID Publish Year Pages File Format Full-Text
2894 141 2015 9 PDF Available
Title
A rapid and simple screening method to identify conditions for enhanced stability of modular vaccine candidates
Abstract

•Modular capsomere presenting rotavirus peptide epitope was unstable in buffer.•DLS analysis was used for HTS of modular capsomere-stability enhancing additives.•High resolution SEC confirmed potential of additives for stabilizing capsomeres.•TX-100, TW-20 and TW-80 were able to enhance the stability of modular capsomeres.

Virus-like particles (VLPs) and capsomere subunits have been developed as safe and effective vaccine candidates in the fight against infectious diseases. These bioengineered structures are suitable platforms for repetitive high density presentation of foreign epitope modules. However, due to the module’s diverse physicochemical properties, modularisation of capsomeres and VLPs requires tailoring of the physicochemical environment specific to each module to maintain protein stability against aggregation. Here, we report a high-throughput technique for screening buffer components to stabilize capsomeres, based on light scattering analysis. This screening method was applied to modular capsomeres presenting peptide epitopes from the rotavirus spike protein VP8 subunit domain, engineered as a next-generation rotavirus vaccine candidate. Among various additives tested, non-ionic detergents, such as Triton X-100, Tween-80 and Tween-20, were able to stabilize modular capsomeres, either alone or in combination with l-arginine, as confirmed with high-resolution size exclusion chromatography. Results demonstrate that tailoring the nature of the environment surrounding self-assembling proteins using small organic molecules can enhance the bioprocessing of modular vaccine capsomeres. The developed screening method potentially provides a powerful approach for rapid tailoring of processing conditions specific to antigenic modules displayed on next-generation recombinant capsomere and VLP vaccines, for low-cost vaccine delivery at global scale.

Keywords
Virus-like particles; Capsomeres; Protein; Aggregation; Downstream processing; Protein recovery
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A rapid and simple screening method to identify conditions for enhanced stability of modular vaccine candidates
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 100, 15 August 2015, Pages 50–58
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us