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2. Packaging protein drugs as bacterial inclusion bodies for therapeutic applications

Author

Villaverde Antonio, García-Fruitós Elena, Rinas Ursula, Seras-Franzoso Joaquin, Kosoy Ana, Corchero José, and Vazquez Esther

Subjects
Microbiology, QR1-502
Abstract

Abstract A growing number of insights on the biology of bacterial inclusion bodies (IBs) have revealed intriguing utilities of these protein particles. Since they combine mechanical stability and protein functionality, IBs have been already exploited in biocatalysis and explored for bottom-up topographical modification in tissue engineering. Being fully biocompatible and with tuneable bio-physical properties, IBs are currently emerging as agents for protein delivery into mammalian cells in protein-replacement cell therapies. So far, IBs formed by chaperones (heat shock protein 70, Hsp70), enzymes (catalase and dihydrofolate reductase), grow factors (leukemia inhibitory factor, LIF) and structural proteins (the cytoskeleton keratin 14) have been shown to rescue exposed cells from a spectrum of stresses and restore cell functions in absence of cytotoxicity. The natural penetrability of IBs into mammalian cells (reaching both cytoplasm and nucleus) empowers them as an unexpected platform for the controlled delivery of essentially any therapeutic polypeptide. Production of protein drugs by biopharma has been traditionally challenged by IB formation. However, a time might have arrived in which recombinant bacteria are to be engineered for the controlled packaging of therapeutic proteins as nanoparticulate materials (nanopills), for their extra- or intra-cellular release in medicine and cosmetics.

Published
2012
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3. Biological activities of histidine-rich peptides; merging biotechnology and nanomedicine

Author

Ferrer-Miralles Neus, Corchero José, Kumar Pradeep, Cedano Juan A, Gupta Kailash C, Villaverde Antonio, and Vazquez Esther

Subjects
Microbiology, QR1-502
Abstract

Abstract Histidine-rich peptides are commonly used in recombinant protein production as purification tags, allowing the one-step affinity separation of the His-tagged proteins from the extracellular media or cell extracts. Genetic engineering makes feasible the post-purification His-tag removal by inserting, between the tag and the main protein body, a target site for trans-acting proteases or a self-proteolytic peptide with regulatable activities. However, for technical ease, His tags are often not removed and the fusion proteins eventually used in this form. In this commentary, we revise the powerful biological properties of histidine-rich peptides as endosomolytic agents and as architectonic tags in nanoparticle formation, for which they are exploited in drug delivery and other nanomedical applications. These activities, generally unknown to biotechnologists, can unwillingly modulate the functionality and biotechnological performance of recombinant proteins in which they remain trivially attached.

Published
2011
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4. Self-assembling, protein-based intracellular bacterial organelles: emerging vehicles for encapsulating, targeting and delivering therapeutical cargoes

Author

Corchero José L and Cedano Juan

Subjects
self-assembling proteins, protein delivery, nanoparticles, Microbiology, QR1-502
Abstract

Abstract Many bacterial species contain intracellular nano- and micro-compartments consisting of self-assembling proteins that form protein-only shells. These structures are built up by combinations of a reduced number of repeated elements, from 60 repeated copies of one unique structural element self-assembled in encapsulins of 24 nm to 10,000-20,000 copies of a few protein species assembled in a organelle of around 100-150 nm in cross-section. However, this apparent simplicity does not correspond to the structural and functional sophistication of some of these organelles. They package, by not yet definitely solved mechanisms, one or more enzymes involved in specific metabolic pathways, confining such reactions and sequestering or increasing the inner concentration of unstable, toxics or volatile intermediate metabolites. From a biotechnological point of view, we can use the self assembling properties of these particles for directing shell assembling and enzyme packaging, mimicking nature to design new applications in biotechnology. Upon appropriate engineering of the building blocks, they could act as a new family of self-assembled, protein-based vehicles in Nanomedicine to encapsulate, target and deliver therapeutic cargoes to specific cell types and/or tissues. This would provide a new, intriguing platform of microbial origin for drug delivery.

Published
2011
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5. Post-production protein stability: trouble beyond the cell factory

Author

Vazquez Esther, Corchero José, and Villaverde Antonio

Subjects
Microbiology, QR1-502
Abstract

Abstract Being protein function a conformation-dependent issue, avoiding aggregation during production is a major challenge in biotechnological processes, what is often successfully addressed by convenient upstream, midstream or downstream approaches. Even when obtained in soluble forms, proteins tend to aggregate, especially if stored and manipulated at high concentrations, as is the case of protein drugs for human therapy. Post-production protein aggregation is then a major concern in the pharmaceutical industry, as protein stability, pharmacokinetics, bioavailability, immunogenicity and side effects are largely dependent on the extent of aggregates formation. Apart from acting at the formulation level, the recombinant nature of protein drugs allows intervening at upstream stages through protein engineering, to produce analogue protein versions with higher stability and enhanced therapeutic values.

Published
2011
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6. Microbial factories for recombinant pharmaceuticals

Author

Domingo-Espín Joan, Ferrer-Miralles Neus, Corchero José, Vázquez Esther, and Villaverde Antonio

Subjects
Microbiology, QR1-502
Abstract

Abstract Most of the hosts used to produce the 151 recombinant pharmaceuticals so far approved for human use by the Food and Drug Administration (FDA) and/or by the European Medicines Agency (EMEA) are microbial cells, either bacteria or yeast. This fact indicates that despite the diverse bottlenecks and obstacles that microbial systems pose to the efficient production of functional mammalian proteins, namely lack or unconventional post-translational modifications, proteolytic instability, poor solubility and activation of cell stress responses, among others, they represent convenient and powerful tools for recombinant protein production. The entering into the market of a progressively increasing number of protein drugs produced in non-microbial systems has not impaired the development of products obtained in microbial cells, proving the robustness of the microbial set of cellular systems (so far Escherichia coli and Saccharomyces cerevisae) developed for protein drug production. We summarize here the nature, properties and applications of all those pharmaceuticals and the relevant features of the current and potential producing hosts, in a comparative way.

Published
2009
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10. Application of Quality by Design to the robust preparation of a liposomal GLA formulation by DELOS-susp method

Author

Merlo-Mas, Josep, Tomsen-Melero, Judit, Corchero, José-Luis, González-Mira, Elisabet, Font, Albert, Pedersen, Jannik N., García-Aranda, Natalia, Cristóbal-Lecina, Edgar, Alcaina-Hernando, Marta, Mendoza, Rosa, Garcia-Fruitós, Elena, Lizarraga, Teresa, Resch, Susanne, Schimpel, Christa, Falk, Andreas, Pulido, Daniel, Royo, Miriam, Schwartz, Simó, Jr., Abasolo, Ibane, Pedersen, Jan Skov, Danino, Dganit, Soldevila, Andreu, Veciana, Jaume, Sala, Santi, Ventosa, Nora, and Córdoba, Alba

Published
2021
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13. Zinc-Assisted Microscale Granules Made of the SARS-CoV-2 Spike Protein Trigger Neutralizing, Antivirus Antibody Responses

Author

Favaro, Marianna T. P., primary, Alamo, Patricia, additional, Roher, Nerea, additional, Chillon, Miguel, additional, Lascorz, Jara, additional, Márquez, Merce, additional, Corchero, José Luis, additional, Mendoza, Rosa, additional, Martínez-Torró, Carlos, additional, Ferrer-Miralles, Neus, additional, Ferreira, Luis C. S., additional, Mangues, Ramón, additional, Vázquez, Esther, additional, Parladé, Eloi, additional, and Villaverde, Antonio, additional

Published
2024
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15. Escherichia coli as a New Platform for the Fast Production of Vault-like Nanoparticles: An Optimized Protocol

Author

Instituto de Salud Carlos III, European Commission, Fundación Mutua Madrileña, Asociación Española Contra el Cáncer, Centro de Investigación Biomédica en Red Bioingeniería, Biomateriales y Nanomedicina (España), Benito, Antoni [0000-0002-9776-1003], Ferrer Miralles, Neus [0000-0003-2981-3913], Céspedes, María Virtudes [0000-0003-2956-5833], Corchero, José Luis [0000-0002-6109-144X], Fernández, Roger, Carreño, Aida, Mendoza, Rosa, Benito, Antoni, Ferrer Miralles, Neus, Céspedes, María Virtudes, Corchero, José Luis, Instituto de Salud Carlos III, European Commission, Fundación Mutua Madrileña, Asociación Española Contra el Cáncer, Centro de Investigación Biomédica en Red Bioingeniería, Biomateriales y Nanomedicina (España), Benito, Antoni [0000-0002-9776-1003], Ferrer Miralles, Neus [0000-0003-2981-3913], Céspedes, María Virtudes [0000-0003-2956-5833], Corchero, José Luis [0000-0002-6109-144X], Fernández, Roger, Carreño, Aida, Mendoza, Rosa, Benito, Antoni, Ferrer Miralles, Neus, Céspedes, María Virtudes, and Corchero, José Luis

Published
2022

16. All-in-one biofabrication and loading of recombinant vaults in human cells

Author

Instituto de Salud Carlos III, Centro de Investigación Biomédica en Red Bioingeniería, Biomateriales y Nanomedicina (España), European Commission, Ministerio de Ciencia, Innovación y Universidades (España), Fundación Mutua Madrileña, Asociación Española Contra el Cáncer, Martín, Fernando [0000-0002-3496-9093], Carreño, Aida [0000-0001-7725-7515], Mendoza, Rosa [0000-0002-0488-4814], Caruana, Pablo [0000-0002-0170-4355], Rodriguez, Francisco [0000-0001-7909-932X], Bravo, Marlon [0000-0002-0065-9812], Benito, Antoni [0000-0002-9776-1003], Ferrer Miralles, Neus [0000-0003-2981-3913], Céspedes, M. Virtudes [0000-0003-2956-5833], Corchero, José Luis [0000-0002-6109-144X], Martín, Fernando, Carreño, Aida, Mendoza, Rosa, Caruana, Pablo, Rodriguez, Francisco, Bravo, Marlon, Benito, Antoni, Ferrer Miralles, Neus, Céspedes, M. Virtudes, Corchero, José Luis, Instituto de Salud Carlos III, Centro de Investigación Biomédica en Red Bioingeniería, Biomateriales y Nanomedicina (España), European Commission, Ministerio de Ciencia, Innovación y Universidades (España), Fundación Mutua Madrileña, Asociación Española Contra el Cáncer, Martín, Fernando [0000-0002-3496-9093], Carreño, Aida [0000-0001-7725-7515], Mendoza, Rosa [0000-0002-0488-4814], Caruana, Pablo [0000-0002-0170-4355], Rodriguez, Francisco [0000-0001-7909-932X], Bravo, Marlon [0000-0002-0065-9812], Benito, Antoni [0000-0002-9776-1003], Ferrer Miralles, Neus [0000-0003-2981-3913], Céspedes, M. Virtudes [0000-0003-2956-5833], Corchero, José Luis [0000-0002-6109-144X], Martín, Fernando, Carreño, Aida, Mendoza, Rosa, Caruana, Pablo, Rodriguez, Francisco, Bravo, Marlon, Benito, Antoni, Ferrer Miralles, Neus, Céspedes, M. Virtudes, and Corchero, José Luis

Abstract

One of the most promising approaches in the drug delivery field is the use of naturally occurring self-assembling protein nanoparticles, such as virus-like particles, bacterial microcompartments or vault ribonucleoprotein particles as drug delivery systems (DDSs). Among them, eukaryotic vaults show a promising future due to their structural features,in vitrostability and non-immunogenicity. Recombinant vaults are routinely produced in insect cells and purified through several ultracentrifugations, both tedious and time-consuming processes. As an alternative, this work proposes a new approach and protocols for the production of recombinant vaults in human cells by transient gene expression of a His-tagged version of the major vault protein (MVP-H6), the development of new affinity-based purification processes for such recombinant vaults, and the all-in-one biofabrication and encapsulation of a cargo recombinant protein within such vaults by their co-expression in human cells. Protocols proposed here allow the easy and straightforward biofabrication and purification of engineered vaults loaded with virtually any INT-tagged cargo protein, in very short times, paving the way to faster and easier engineering and production of better and more efficient DDS.

Published
2022

17. Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview

Author

Corchero, José Luis, primary, Favaro, Marianna T. P., additional, Márquez-Martínez, Merce, additional, Lascorz, Jara, additional, Martínez-Torró, Carlos, additional, Sánchez, Julieta M., additional, López-Laguna, Hèctor, additional, de Souza Ferreira, Luís Carlos, additional, Vázquez, Esther, additional, Ferrer-Miralles, Neus, additional, Villaverde, Antonio, additional, and Parladé, Eloi, additional

Published
2023
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27. Nano-Based Approved Pharmaceuticals for Cancer Treatment: Present and Future Challenges

Author

Rodríguez, Francisco, primary, Caruana, Pablo, additional, De la Fuente, Noa, additional, Español, Pía, additional, Gámez, María, additional, Balart, Josep, additional, Llurba, Elisa, additional, Rovira, Ramón, additional, Ruiz, Raúl, additional, Martín-Lorente, Cristina, additional, Corchero, José Luis, additional, and Céspedes, María Virtudes, additional

Published
2022
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28. Liposomes and its use for enzyme delivery

Author

Ventosa, Leonor, Veciana, Jaume, Royo, Miriam, Tomsen Melero, Judit, Abasolo, Ibane, Schwartz Jr., Simó, Corchero, José Luis, Pulido, Daniel, Cristóbal Lecina, Edgar, González Mira, Elisabet, Sala Vergés, Santiago, Córdoba, Alba, Merlo Mas, Josep, Soldevila, Andreu, Font, Albert, Ventosa, Leonor, Veciana, Jaume, Royo, Miriam, Tomsen Melero, Judit, Abasolo, Ibane, Schwartz Jr., Simó, Corchero, José Luis, Pulido, Daniel, Cristóbal Lecina, Edgar, González Mira, Elisabet, Sala Vergés, Santiago, Córdoba, Alba, Merlo Mas, Josep, Soldevila, Andreu, and Font, Albert

Abstract

The present invention refers to a liposome comprising: a) a phospholipid; b) cholesterol (chol); c) a conjugate comprising a cholesterol moiety, a polyethylene glycol (PEG) moiety and a peptide moiety comprising a RGD sequence, wherein the PEG moiety is covalently attached to the cholesterol moiety by one end via a bond of the type alkyl ether and is covalently attached to the peptide moiety comprising the RGD sequence by the other end: d) a non-lipid cationic surfactant present in a percentage of less than 30% mol in respect to the total mol of the components of the liposome a), b), c) and d); and e) alpha-galactosidase (GLA) enzyme present in a ratio of micrograms of GLA in respect to the total milligrams of the components of the liposome a), b), c) and d) of between and including 2 to 35. It also refers to a pharmaceutical composition that comprises it and to the liposome or the pharmaceutical composition for use as a medicament, in particular for use in the treatment of Fabry disease. It also refers to a process for the production of the liposome.

Published
2022

30. α-Galactosidase-A Loaded-Nanoliposomes with Enhanced Enzymatic Activity and Intracellular Penetration

Author

Cabrera, Ingrid, Abasolo, Ibane, Corchero, José L., Elizondo, Elisa, Gil, Pilar Rivera, Moreno, Evelyn, Faraudo, Jordi, Sala, Santi, Bueno, Dolores, González-Mira, Elisabet, Rivas, Merche, Melgarejo, Marta, Pulido, Daniel, Albericio, Fernando, Royo, Miriam, Villaverde, Antonio, García-Parajo, Maria F., Schwartz, Simó, Jr., Ventosa, Nora, and Veciana, Jaume

Published
2016
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31. Efficacy of targeted nanoliposomes in reducing globotriaosylceramide (Gb3) accumulation in mouse models of Fabry disease

Author

Moltó-Abad, Marc, primary, Riascos, Zamira-V Díaz, additional, Tomsen-Melero, Judit, additional, González-Mira, Elisabet, additional, Casas, Josefina, additional, Cristóbal-Lecina, Edgar, additional, Font, Albert, additional, Corchero, José Luis, additional, Pulido, Daniel, additional, Soldevila, Andreu, additional, Royo, Miriam, additional, Córdoba, Alba, additional, Merlo-Mas, Josep, additional, Ferrer, Lidia, additional, Sala, Santi, additional, Mancilla-Zamora, Sandra, additional, Llaguno-Munive, Monserrat, additional, Zamora-Pérez, Paula, additional, Garcia-Prats, Belén, additional, Ventosa, Nora, additional, and Abasolo, Ibane, additional

Published
2022
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34. Biomedical Applications of Bacterial Inclusion Bodies

Author

Ratera, Imma, primary, Peternel, Spela, additional, Seras-Franzoso, Joaquin, additional, Cano-Garrido, Olivia, additional, García-Fruitós, Elena, additional, Cubarsí, Rafael, additional, Vazquez, Esther, additional, Corchero, José Luis, additional, Rodríguez-Carmona, Escarlata, additional, Veciana, Jaume, additional, and Villaverde, Antonio, additional

Published
2014
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36. Liposomas funcionalizados útiles para la administración de compuestos bioactivos

Author

Veciana, Jaume [0000-0003-1023-9923], Royo, Miriam [0000-0001-5292-0819], Pulido, Daniel [0000-0002-2841-194X], Corchero, José Luis [0000-0002-6109-144X], Schwartz Jr., Simó [0000-0001-8297-7971], Abasolo, Ibane [0000-0001-5970-6276], Ventosa, Nora, Veciana, Jaume, Cabrera, Ingrid, Elizondo, Elisa, Melgarejo Díaz, Marta, Royo, Miriam, Albericio, Fernando, Pulido, Daniel, Sala Vergés, Santiago, Corchero, José Luis, Schwartz Jr., Simó, Abasolo, Ibane, Villaverde Corrales, Antonio Pedro, Veciana, Jaume [0000-0003-1023-9923], Royo, Miriam [0000-0001-5292-0819], Pulido, Daniel [0000-0002-2841-194X], Corchero, José Luis [0000-0002-6109-144X], Schwartz Jr., Simó [0000-0001-8297-7971], Abasolo, Ibane [0000-0001-5970-6276], Ventosa, Nora, Veciana, Jaume, Cabrera, Ingrid, Elizondo, Elisa, Melgarejo Díaz, Marta, Royo, Miriam, Albericio, Fernando, Pulido, Daniel, Sala Vergés, Santiago, Corchero, José Luis, Schwartz Jr., Simó, Abasolo, Ibane, and Villaverde Corrales, Antonio Pedro

Abstract

Un conjugado, que comprende: i) un esterol; ii) una cadena de polietilenglicol que tiene un extremo proximal y un extremo distal, en el que dicha cadena de polietilenglicol está unida covalentemente por su extremo proximal a i) mediante un enlace de tipo alquil éter; iii) un péptido, capaz de unirse selectivamente a uno o varios receptores presentes en una célula diana, estando dicho péptido unido covalentemente al extremo distal de ii).

Published
2019

37. Liposomes et leur utilisation pour l'administration d'enzymes

Author

Ventosa, Leonor, Veciana, Jaume, Royo, Miriam, Tomsen Melero, Judit, Abasolo, Ibane, Schwartz Jr., Simó, Corchero, José Luis, Pulido, Daniel, Cristóbal Lecina, Edgar, González Mira, Elisabet, Sala Vergés, Santiago, Córdoba, Alba, Merlo Mas, Josep, Soldevila, Andreu, and Font, Albert

Abstract

[EN] The present invention refers to a liposome comprising: a) a phospholipid; b) cholesterol (chol); c) a conjugate comprising a cholesterol moiety, a polyethylene glycol (PEG) moiety and a peptide moiety comprising a RGD sequence, wherein the PEG moiety is covalently attached to the cholesterol moiety by one end via a bond of the type alkyl ether and is covalently attached to the peptide moiety comprising the RGD sequence by the other end: d) a non-lipid cationic surfactant present in a percentage of less than 30% mol in respect to the total mol of the components of the liposome a), b), c) and d); and e) alpha-galactosidase (GLA) enzyme present in a ratio of micrograms of GLA in respect to the total milligrams of the components of the liposome a), b), c) and d) of between and including 2 to 35. It also refers to a pharmaceutical composition that comprises it and to the liposome or the pharmaceutical composition for use as a medicament, in particular for use in the treatment of Fabry disease. It also refers to a process for the production of the liposome., [FR] La présente invention concerne un liposome comprenant : a) un phospholipide ; b) cholestérol (chol) ; c) un conjugué comprenant une fraction de cholestérol, une fraction de polyéthylène glycol (PEG) et une fraction peptidique comprenant une séquence RGD, la fraction PEG étant liée de manière covalente à la fraction de cholestérol par une extrémité par l'intermédiaire d'une liaison du type éther alcoylique et étant liée de manière covalente à la fraction peptidique comprenant la séquence RGD par l'autre extrémité : d) un agent tensioactif cationique non lipidique présent dans un pourcentage inférieur à 30% molaire par rapport au total molaire des composants du liposome a), b), c) et d) ; et e) l'enzyme alpha-galactosidase (GLA) présente dans un rapport de microgrammes de GLA par rapport aux milligrammes totaux des composants du liposome a), b), c) et d) de 2 à 35 inclus. L'invention concerne également une composition pharmaceutique qui le comprend et le liposome ou la composition pharmaceutique pour une utilisation comme médicament, en particulier pour une utilisation dans le traitement de la maladie de Fabry. L'invention concerne également un procédé de production du liposome., Consejo Superior de Investigaciones Científicas (CSIC), Consorcio Centro de Investigación Biomédica En Red, Fundació Hospital Universitari Vall D'Hebron - Institut de Recerca, Nanomol Technologies, S.L., Leanbio, A1 Solicitud de patente con informe sobre el estado de la técnica

Published
2021

39. Citrate-Assisted Regulation of Protein Stability and Secretability from Synthetic Amyloids

Author

López-Laguna, Hèctor, Favaro, Marianna T.P., Chellou-Bakkali, Sara, Voltà-Durán, Eric, Parladé, Eloi, Sánchez, Julieta, Corchero, José Luis, Unzueta, Ugutz, Villaverde, Antonio, and Vázquez, Esther

Abstract

The mammalian endocrine system uses functional amyloids as dynamic depots to store and release protein hormones into the bloodstream. Such depots, acting as secretory granules within the microscale, are formed in specialized cells by the coordination between the ionic, divalent form of zinc (Zn2+) and the imidazole ring from accessible His residues. The reversibility of such cross-linking events allows for the release of monomeric or oligomeric forms of the functional protein for biological activity. In vitro, and mimicking such a natural coordination process, synthetic amyloidal granules with secretory properties can be fabricated using selected therapeutic proteins as building blocks. Then, these microparticles act as delivery systems for endocrine-like, sustained protein release, with proven applicability in vaccinology, cancer therapy, regenerative medicine, and as antimicrobial agents. While the temporal profile in which the protein is leaked from the material might be highly relevant to clinically oriented applications, the fine control of such parameters remains unclear. We have explored here how the kinetics of protein release can be regulated by intervening in the storage formulation of the granules, through the concentration of citrate not only as a buffer component and protein stabilizer but also as a chelating agent. The citrate-assisted, time-prolonged regulatable release of proteins, in their functional form, opens a spectrum of possibilities to adjust the preparation of synthetic secretory granules to specific clinical needs.

Published
2025
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40. Extracellular vesicles from recombinant cell factories improve the activity and efficacy of enzymes defective in lysosomal storage disorders

Author

Seras‐Franzoso, Joaquin, Díaz‐Riascos, Zamira V., Corchero, José Luis, González, Patricia, García-Aranda, Natalia, Mandaña, Mònica, Riera, Roger, Boullosa, Ana, Mancila, Sandra, Grayston, Alba, Moltó-Abad, Marc, Mendoza, Rosa, Garcia‐Fruitós, Elena, Pintos‐Morell, Guillem, Albertazzi, Lorenzo, Rosell, Anna, Casas, Josefina, Villaverde, Antonio, Schwartz Jr., Simó, Abasolo, Ibane, Seras‐Franzoso, Joaquin, Díaz‐Riascos, Zamira V., Corchero, José Luis, González, Patricia, García-Aranda, Natalia, Mandaña, Mònica, Riera, Roger, Boullosa, Ana, Mancila, Sandra, Grayston, Alba, Moltó-Abad, Marc, Mendoza, Rosa, Garcia‐Fruitós, Elena, Pintos‐Morell, Guillem, Albertazzi, Lorenzo, Rosell, Anna, Casas, Josefina, Villaverde, Antonio, Schwartz Jr., Simó, and Abasolo, Ibane

Abstract

In the present study the use of extracellular vesicles (EVs) as vehicles for therapeutic enzymes in lysosomal storage disorders was explored. EVs were isolated from mammalian cells overexpressing alpha‐galactosidase A (GLA) or N‐sulfoglucosamine sulfohydrolase (SGSH) enzymes, defective in Fabry and Sanfilippo A diseases, respectively. Direct purification of EVs from cell supernatants was found to be a simple and efficient method to obtain highly active GLA and SGSH proteins, even after EV lyophilization. Likewise, EVs carrying GLA (EV‐GLA) were rapidly uptaken and reached the lysosomes in cellular models of Fabry disease, restoring lysosomal functionality much more efficiently than the recombinant enzyme in clinical use. In vivo, EVs were well tolerated and distributed among all main organs, including the brain. DiR‐labelled EVs were localized in brain parenchyma 1 h after intra‐arterial (internal carotid artery) or intravenous (tail vein) administrations. Moreover, a single intravenous administration of EV‐GLA was able to reduce globotriaosylceramide (Gb3) substrate levels in clinically relevant tissues, such kidneys and brain. Overall, our results demonstrate that EVs from cells overexpressing lysosomal enzymes act as natural protein delivery systems, improving the activity and the efficacy of the recombinant proteins and facilitating their access to organs neglected by conventional enzyme replacement therapies.

Published
2021

41. Extracellular vesicles from recombinant cell factories improve the activity and efficacy of enzymes defective in lysosomal storage disorders

Author

Seras‐Franzoso, Joaquin, primary, Díaz‐Riascos, Zamira V., additional, Corchero, José Luis, additional, González, Patricia, additional, García‐Aranda, Natalia, additional, Mandaña, Mònica, additional, Riera, Roger, additional, Boullosa, Ana, additional, Mancilla, Sandra, additional, Grayston, Alba, additional, Moltó‐Abad, Marc, additional, Garcia‐Fruitós, Elena, additional, Mendoza, Rosa, additional, Pintos‐Morell, Guillem, additional, Albertazzi, Lorenzo, additional, Rosell, Anna, additional, Casas, Josefina, additional, Villaverde, Antonio, additional, Schwartz, Simó, additional, and Abasolo, Ibane, additional

Published
2021
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44. Impact of Chemical Composition on the Nanostructure and Biological Activity of α-Galactosidase-Loaded Nanovesicles for Fabry Disease Treatment

Author

Tomsen-Melero, Judit, primary, Passemard, Solène, additional, García-Aranda, Natalia, additional, Díaz-Riascos, Zamira Vanessa, additional, González-Rioja, Ramon, additional, Nedergaard Pedersen, Jannik, additional, Lyngsø, Jeppe, additional, Merlo-Mas, Josep, additional, Cristóbal-Lecina, Edgar, additional, Corchero, José Luis, additional, Pulido, Daniel, additional, Cámara-Sánchez, Patricia, additional, Portnaya, Irina, additional, Ionita, Inbal, additional, Schwartz, Simó, additional, Veciana, Jaume, additional, Sala, Santi, additional, Royo, Miriam, additional, Córdoba, Alba, additional, Danino, Dganit, additional, Pedersen, Jan Skov, additional, González-Mira, Elisabet, additional, Abasolo, Ibane, additional, and Ventosa, Nora, additional

Published
2021
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48. Scale-up and Quality by Design application to the robust production of an enzyme-loaded liposomal formulation by DELOS-susp method

Author

Merlo, Josep, primary, Tomsen-Melero, Judit, additional, Corchero, José-Luis, additional, González-Mira, Elisabet, additional, Font, Albert, additional, Pedersen, Jannik N., additional, García-Aranda, Natalia, additional, Cristóbal-Lecina, Edgar, additional, Royo, Míriam, additional, Abasolo, Ibane, additional, Pedersen, Jan S., additional, Danino, Dganit, additional, Soldevila, Andreu, additional, Sala, Santi, additional, Ventosa, Nora, additional, and Córdoba, Alba, additional

Published
2020
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49. Functionalized liposomes useful for the delivery of bioactive compounds

Author

Veciana, Jaume [0000-0003-1023-9923], Royo, Miriam [0000-0001-5292-0819], Pulido, Daniel [0000-0002-2841-194X], Corchero, José Luis [0000-0002-6109-144X], Schwartz Jr., Simó [0000-0001-8297-7971], Abasolo, Ibane [0000-0001-5970-6276], Ventosa, Nora, Veciana, Jaume, Cabrera, Ingrid, Elizondo, Elisa, Melgarejo Díaz, Marta, Royo, Miriam, Albericio, Fernando, Pulido, Daniel, Sala Vergés, Santiago, Corchero, José Luis, Schwartz Jr., Simó, Abasolo, Ibane, Villaverde Corrales, Antonio Pedro, Veciana, Jaume [0000-0003-1023-9923], Royo, Miriam [0000-0001-5292-0819], Pulido, Daniel [0000-0002-2841-194X], Corchero, José Luis [0000-0002-6109-144X], Schwartz Jr., Simó [0000-0001-8297-7971], Abasolo, Ibane [0000-0001-5970-6276], Ventosa, Nora, Veciana, Jaume, Cabrera, Ingrid, Elizondo, Elisa, Melgarejo Díaz, Marta, Royo, Miriam, Albericio, Fernando, Pulido, Daniel, Sala Vergés, Santiago, Corchero, José Luis, Schwartz Jr., Simó, Abasolo, Ibane, and Villaverde Corrales, Antonio Pedro

Abstract

The present invention is related to new functionalized liposomes for the selective delivery of active agents. These liposomes, dueto theirfunctionalization with multiple guiding ligands, m ay have potential applications in cosmetics and therapy.

Published
2018

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