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Stability Studies of the Vaccine Adjuvant U-Omp19

Unlipidated outer membrane protein 19 (U-Omp19) is a novel mucosal adjuvant in preclinical development to be used in vaccine formulations. U-Omp19 holds two main properties, it is capable of inhibiting gastrointestinal and lysosomal peptidases, increasing the amount of co-administered antigen that r...

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Autores principales: Darriba, M. Laura, Cerutti, María L., Bruno, Laura, Cassataro, Juliana, Pasquevich, Karina A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7815325/
https://www.ncbi.nlm.nih.gov/pubmed/33058898
http://dx.doi.org/10.1016/j.xphs.2020.10.011
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author Darriba, M. Laura
Cerutti, María L.
Bruno, Laura
Cassataro, Juliana
Pasquevich, Karina A.
author_facet Darriba, M. Laura
Cerutti, María L.
Bruno, Laura
Cassataro, Juliana
Pasquevich, Karina A.
author_sort Darriba, M. Laura
collection PubMed
description Unlipidated outer membrane protein 19 (U-Omp19) is a novel mucosal adjuvant in preclinical development to be used in vaccine formulations. U-Omp19 holds two main properties, it is capable of inhibiting gastrointestinal and lysosomal peptidases, increasing the amount of co-administered antigen that reaches the immune inductive sites and its half-life inside cells, and it is able to stimulate antigen presenting cells in vivo. These activities enable U-Omp19 to enhance the adaptive immune response to co-administrated antigens. To characterize the stability of U-Omp19 we have performed an extensive analysis of its physicochemical and biological properties in a 3-year long-term stability study, and under potentially damaging freeze-thawing and lyophilization stress processes. Results revealed that U-Omp19 retains its full protease inhibitor activity, its monomeric state and its secondary structure even when stored in solution for 36 months or after multiple freeze-thawing cycles. Non-enzymatic hydrolysis resulted the major degradation pathway for storage in solution at 4 °C or room temperature which can be abrogated by lyophilization yet increasing protein tendency to form aggregates. This information will play a key role in the development of a stable formulation of U-Omp19, allowing an extended shelf-life during manufacturing, storage, and shipping of a future vaccine containing this pioneering adjuvant.
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spelling pubmed-78153252021-02-01 Stability Studies of the Vaccine Adjuvant U-Omp19 Darriba, M. Laura Cerutti, María L. Bruno, Laura Cassataro, Juliana Pasquevich, Karina A. J Pharm Sci Research Article Unlipidated outer membrane protein 19 (U-Omp19) is a novel mucosal adjuvant in preclinical development to be used in vaccine formulations. U-Omp19 holds two main properties, it is capable of inhibiting gastrointestinal and lysosomal peptidases, increasing the amount of co-administered antigen that reaches the immune inductive sites and its half-life inside cells, and it is able to stimulate antigen presenting cells in vivo. These activities enable U-Omp19 to enhance the adaptive immune response to co-administrated antigens. To characterize the stability of U-Omp19 we have performed an extensive analysis of its physicochemical and biological properties in a 3-year long-term stability study, and under potentially damaging freeze-thawing and lyophilization stress processes. Results revealed that U-Omp19 retains its full protease inhibitor activity, its monomeric state and its secondary structure even when stored in solution for 36 months or after multiple freeze-thawing cycles. Non-enzymatic hydrolysis resulted the major degradation pathway for storage in solution at 4 °C or room temperature which can be abrogated by lyophilization yet increasing protein tendency to form aggregates. This information will play a key role in the development of a stable formulation of U-Omp19, allowing an extended shelf-life during manufacturing, storage, and shipping of a future vaccine containing this pioneering adjuvant. Elsevier 2021-02 /pmc/articles/PMC7815325/ /pubmed/33058898 http://dx.doi.org/10.1016/j.xphs.2020.10.011 Text en © 2020 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Research Article
Darriba, M. Laura
Cerutti, María L.
Bruno, Laura
Cassataro, Juliana
Pasquevich, Karina A.
Stability Studies of the Vaccine Adjuvant U-Omp19
title Stability Studies of the Vaccine Adjuvant U-Omp19
title_full Stability Studies of the Vaccine Adjuvant U-Omp19
title_fullStr Stability Studies of the Vaccine Adjuvant U-Omp19
title_full_unstemmed Stability Studies of the Vaccine Adjuvant U-Omp19
title_short Stability Studies of the Vaccine Adjuvant U-Omp19
title_sort stability studies of the vaccine adjuvant u-omp19
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7815325/
https://www.ncbi.nlm.nih.gov/pubmed/33058898
http://dx.doi.org/10.1016/j.xphs.2020.10.011
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