Stability Studies of the Vaccine Adjuvant U-Omp19

Autores
Darriba, Maria Laura; Cerutti, Maria Laura; Bruno, Laura Alejandra; Cassataro, Juliana; Pasquevich, Karina Alejandra
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Darriba, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Cerutti, Maria Laura. Universidad Nacional de San Martin. Centro de Rediseño E Ingenieria de Proteinas.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Bruno, Laura Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Cassataro, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Pasquevich, Karina Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Materia
ANALYTICAL BIOCHEMISTRY
CIRCULAR DICHROISM
LIGHT SCATTERING (DYNAMIC)
LYOPHILIZATION
MUCOSAL IMMUNIZATION
MUCOSAL VACCINATION
ORAL DRUG DELIVERY
PHYSICOCHEMICAL PROPERTIES
PREFORMULATION
PROTEASE
PROTEIN AGGREGATION
PROTEIN FORMULATION
STABILITY
VACCINE ADJUVANTS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/153777
Acceder
id CONICETDig_edbe82125ecc32377b3c7fc604825316
oai_identifier_str oai:ri.conicet.gov.ar:11336/153777
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Stability Studies of the Vaccine Adjuvant U-Omp19Darriba, Maria LauraCerutti, Maria LauraBruno, Laura AlejandraCassataro, JulianaPasquevich, Karina AlejandraANALYTICAL BIOCHEMISTRYCIRCULAR DICHROISMLIGHT SCATTERING (DYNAMIC)LYOPHILIZATIONMUCOSAL IMMUNIZATIONMUCOSAL VACCINATIONORAL DRUG DELIVERYPHYSICOCHEMICAL PROPERTIESPREFORMULATIONPROTEASEPROTEIN AGGREGATIONPROTEIN FORMULATIONSTABILITYVACCINE ADJUVANTShttps://purl.org/becyt/ford/3.4https://purl.org/becyt/ford/3https://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Unlipidated 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.Fil: Darriba, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Cerutti, Maria Laura. Universidad Nacional de San Martin. Centro de Rediseño E Ingenieria de Proteinas.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Bruno, Laura Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Cassataro, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Pasquevich, Karina Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaJohn Wiley & Sons Inc.2021-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/153777Darriba, Maria Laura; Cerutti, Maria Laura; Bruno, Laura Alejandra; Cassataro, Juliana; Pasquevich, Karina Alejandra; Stability Studies of the Vaccine Adjuvant U-Omp19; John Wiley & Sons Inc.; Journal of Pharmaceutical Sciences; 110; 2; 2-2021; 707-7180022-35491520-6017CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0022354920306006info:eu-repo/semantics/altIdentifier/doi/10.1016/j.xphs.2020.10.011info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:30:19Zoai:ri.conicet.gov.ar:11336/153777instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:30:20.049CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Stability Studies of the Vaccine Adjuvant U-Omp19
title Stability Studies of the Vaccine Adjuvant U-Omp19
spellingShingle Stability Studies of the Vaccine Adjuvant U-Omp19
Darriba, Maria Laura
ANALYTICAL BIOCHEMISTRY
CIRCULAR DICHROISM
LIGHT SCATTERING (DYNAMIC)
LYOPHILIZATION
MUCOSAL IMMUNIZATION
MUCOSAL VACCINATION
ORAL DRUG DELIVERY
PHYSICOCHEMICAL PROPERTIES
PREFORMULATION
PROTEASE
PROTEIN AGGREGATION
PROTEIN FORMULATION
STABILITY
VACCINE ADJUVANTS
title_short 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_sort Stability Studies of the Vaccine Adjuvant U-Omp19
dc.creator.none.fl_str_mv Darriba, Maria Laura
Cerutti, Maria Laura
Bruno, Laura Alejandra
Cassataro, Juliana
Pasquevich, Karina Alejandra
author Darriba, Maria Laura
author_facet Darriba, Maria Laura
Cerutti, Maria Laura
Bruno, Laura Alejandra
Cassataro, Juliana
Pasquevich, Karina Alejandra
author_role author
author2 Cerutti, Maria Laura
Bruno, Laura Alejandra
Cassataro, Juliana
Pasquevich, Karina Alejandra
author2_role author
author
author
author
dc.subject.none.fl_str_mv ANALYTICAL BIOCHEMISTRY
CIRCULAR DICHROISM
LIGHT SCATTERING (DYNAMIC)
LYOPHILIZATION
MUCOSAL IMMUNIZATION
MUCOSAL VACCINATION
ORAL DRUG DELIVERY
PHYSICOCHEMICAL PROPERTIES
PREFORMULATION
PROTEASE
PROTEIN AGGREGATION
PROTEIN FORMULATION
STABILITY
VACCINE ADJUVANTS
topic ANALYTICAL BIOCHEMISTRY
CIRCULAR DICHROISM
LIGHT SCATTERING (DYNAMIC)
LYOPHILIZATION
MUCOSAL IMMUNIZATION
MUCOSAL VACCINATION
ORAL DRUG DELIVERY
PHYSICOCHEMICAL PROPERTIES
PREFORMULATION
PROTEASE
PROTEIN AGGREGATION
PROTEIN FORMULATION
STABILITY
VACCINE ADJUVANTS
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.4
https://purl.org/becyt/ford/3
https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv 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.
Fil: Darriba, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Cerutti, Maria Laura. Universidad Nacional de San Martin. Centro de Rediseño E Ingenieria de Proteinas.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Bruno, Laura Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Cassataro, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Pasquevich, Karina Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
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.
publishDate 2021
dc.date.none.fl_str_mv 2021-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/153777
Darriba, Maria Laura; Cerutti, Maria Laura; Bruno, Laura Alejandra; Cassataro, Juliana; Pasquevich, Karina Alejandra; Stability Studies of the Vaccine Adjuvant U-Omp19; John Wiley & Sons Inc.; Journal of Pharmaceutical Sciences; 110; 2; 2-2021; 707-718
0022-3549
1520-6017
CONICET Digital
CONICET
url http://hdl.handle.net/11336/153777
identifier_str_mv Darriba, Maria Laura; Cerutti, Maria Laura; Bruno, Laura Alejandra; Cassataro, Juliana; Pasquevich, Karina Alejandra; Stability Studies of the Vaccine Adjuvant U-Omp19; John Wiley & Sons Inc.; Journal of Pharmaceutical Sciences; 110; 2; 2-2021; 707-718
0022-3549
1520-6017
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0022354920306006
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.xphs.2020.10.011
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv John Wiley & Sons Inc.
publisher.none.fl_str_mv John Wiley & Sons Inc.
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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