dc.creator | Carratalá, Jose V. | |
dc.creator | Brouillette, Eric | |
dc.creator | Serna, Naroa | |
dc.creator | Sánchez-Chardi, Alejandro | |
dc.creator | Sanchez, Julieta Maria | |
dc.creator | Villaverde, Antonio | |
dc.creator | Arís, Anna | |
dc.creator | Garcia-Fruitós, Elena | |
dc.creator | Ferrer-Miralles, Neus | |
dc.creator | Malouin, François | |
dc.date.accessioned | 2021-06-15T18:34:58Z | |
dc.date.accessioned | 2022-10-15T14:38:50Z | |
dc.date.available | 2021-06-15T18:34:58Z | |
dc.date.available | 2022-10-15T14:38:50Z | |
dc.date.created | 2021-06-15T18:34:58Z | |
dc.date.issued | 2020-12 | |
dc.identifier | Carratalá, Jose V.; Brouillette, Eric; Serna, Naroa; Sánchez-Chardi, Alejandro; Sanchez, Julieta Maria; et al.; In vivo bactericidal efficacy of gwh1 antimicrobial peptide displayed on protein nanoparticles, a potential alternative to antibiotics; MDPI AG; Pharmaceutics; 12; 12; 12-2020; 1-16 | |
dc.identifier | http://hdl.handle.net/11336/133929 | |
dc.identifier | 1999-4923 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4397847 | |
dc.description.abstract | Oligomerization of antimicrobial peptides into nanosized supramolecular complexes produced in biological systems (inclusion bodies and self-assembling nanoparticles) seems an appealing alternative to conventional antibiotics. In this work, the antimicrobial peptide, GWH1, was N-terminally fused to two different scaffold proteins, namely, GFP and IFN-γ for its bacterial production in the form of such recombinant protein complexes. Protein self-assembling as regular soluble protein nanoparticles was achieved in the case of GWH1-GFP, while oligomerization into bacterial inclusion bodies was reached in both constructions. Among all these types of therapeutic proteins, protein nanoparticles of GWH1-GFP showed the highest bactericidal effect in an in vitro assay against Escherichia coli, whereas non-oligomerized GWH1-GFP and GWH1-IFN-γ only displayed a moderate bactericidal activity. These results indicate that the biological activity of GWH1 is specifically enhanced in the form of regular multi-display configurations. Those in vitro observations were fully validated against a bacterial infection using a mouse mastitis model, in which the GWH1-GFP soluble nanoparticles were able to effectively reduce bacterial loads. | |
dc.language | eng | |
dc.publisher | MDPI AG | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3390/pharmaceutics12121217 | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1999-4923/12/12/1217 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | ANTIMICROBIAL PEPTIDE | |
dc.subject | ESCHERICHIA COLI | |
dc.subject | INCLUSION BODY | |
dc.subject | MOUSE MASTITIS MODEL | |
dc.subject | PROTEIN NANOPARTICLE | |
dc.subject | RECOMBINANT PROTEIN | |
dc.subject | STAPHYLOCOCCUS AUREUS | |
dc.subject | THERAPEUTIC PROTEIN | |
dc.title | In vivo bactericidal efficacy of gwh1 antimicrobial peptide displayed on protein nanoparticles, a potential alternative to antibiotics | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |