Web of Science: 2 citas, Scopus: 2 citas, Google Scholar: citas,
Aggregation-prone peptides modulate activity of bovine interferon gamma released from naturally occurring protein nanoparticles
Carratalá, José Vicente (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Cano Garrido, Olivia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Sánchez, Julieta María (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Membrado, Cristina (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Pérez, Eudald (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Conchillo-Solé, Oscar (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Daura i Ribera, Xavier (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Sánchez Chardi, Alejandro (Universitat Autònoma de Barcelona. Servei de Microscòpia)
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)
Arís i Giralt, Anna (Institut de Recerca i Tecnologia Agroalimentàries)
García Fruitós, Elena (Institut de Recerca i Tecnologia Agroalimentàries)
Ferrer Miralles, Neus (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")

Fecha: 2020
Resumen: Efficient protocols for the production of recombinant proteins are indispensable for the development of the biopharmaceutical sector. Accumulation of recombinant proteins in naturally-occurring protein aggregates is detrimental to biopharmaceutical development. In recent years, the view of protein aggregates has changed with the recognition that they are a valuable source of functional recombinant proteins. In this study, bovine interferon-gamma (rBoIFN-γ) was engineered to enhance the formation of protein aggregates, also known as protein nanoparticles (NPs), by the addition of aggregation-prone peptides (APPs) in the generally recognized as safe (GRAS) bacterial Lactococcus lactis expression system. The L6K2, HALRU and CYOB peptides were selected to assess their intrinsic aggregation capability to nucleate protein aggregation. These APPs enhanced the tendency of the resulting protein to aggregate at the expense of total protein yield. However, fine physico-chemical characterization of the resulting intracellular protein NPs, the protein released from them and the protein purified from the soluble cell fraction indicated that the compactability of protein conformations was directly related to the biological activity of variants of IFN-γ, used here as a model protein with therapeutic potential. APPs enhanced the aggregation tendency of fused rBoIFN-γ while increasing compactability of protein species. Biological activity of rBoIFN-γ was favored in more compacted conformations. Naturally-occurring protein aggregates can be produced in GRAS microorganisms as protein depots of releasable active protein. The addition of APPs to enhance the aggregation tendency has a positive impact in overall compactability and functionality of resulting protein conformers.
Nota: Número d'acord de subvenció MINECO/RTA2015-00064-C02-01
Nota: Número d'acord de subvenció MINECO/RTA2015-00064-C02-02
Nota: Número d'acord de subvenció AGAUR/2017/SGR-229
Derechos: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades. Creative Commons
Lengua: Anglès
Documento: article ; recerca ; submittedVersion ; acceptedVersion
Materia: Interferon-gamma ; Protein nanoparticles ; Protein aggregation ; Lactococcus lactis ; Generally recognized as safe ; Conformational compactability
Publicado en: New Biotechnolgy, Vol. 57 (July 2020) , p. 11-19, ISSN 1871-6784

DOI: 10.1016/j.nbt.2020.02.001


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El registro aparece en las colecciones:
Documentos de investigación > Documentos de los grupos de investigación de la UAB > Centros y grupos de investigación (producción científica) > Ciencias de la salud y biociencias > Instituto de Biotecnología y de Biomedicina (IBB)
Artículos > Artículos de investigación
Artículos > Artículos publicados

 Registro creado el 2020-02-21, última modificación el 2020-08-30



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