ArticleMolecular pharmaceutics2015
Design and characterization of novel recombinant listeriolysin O-protamine fusion proteins for enhanced gene delivery.
Article in Molecular pharmaceutics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Recombinant listeriolysin-O as a platform for next-generation vaccines: Mechanisms, immunological evidence, and translational applications in human and veterinary medicine.Open veterinary journal · 2026Review
- Mesenchymal Stem Cell-Derived Extracellular Vesicles: Seeking into Cell-Free Therapies for Bone-Affected Lysosomal Storage Disorders.International journal of molecular sciences · 2025Review
- Revival of Bioengineered Proteins as Carriers for Nucleic Acids.Bioconjugate chemistry · 2024Article
- Protein-based nanoparticles for therapeutic nucleic acid delivery.Biomaterials · 2024Review
- Peptide-Assisted Nucleic Acid Delivery Systems on the Rise.International journal of molecular sciences · 2021Review
- Biopolymer-based Carriers for DNA Vaccine Design.Angewandte Chemie (International ed. in English) · 2021Review
- Gene delivery by peptide-assisted transport.Current opinion in biomedical engineering · 2018Article
- Intracellular oligonucleotide delivery using the cell penetrating peptide Xentry.Scientific reports · 2018Article
- The Comparative Utility of Viromer RED and Lipofectamine for Transient Gene Introduction into Glial Cells.BioMed research international · 2015Article
- A Novel Strategy for Enhance Potentiation of Meglumine antimoniate againstIranian journal of parasitologyArticle
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To improve the efficiency of gene delivery for effective gene therapy, it is essential that the vector carries functional components that can promote overcoming barriers in various steps leading to the transport of DNA from extracellular to ultimately nuclear compartment. In this study, we designed genetically engineered fusion proteins as a platform to incorporate multiple functionalities in one chimeric protein. Prototypes of such a chimera tested here contain two domains: one that binds to DNA; the other that can facilitate endosomal escape of DNA. The fusion proteins are composed of listeriolysin O (LLO), the endosomolytic pore-forming protein from Listeria monocytogenes, and a 22 amino acid sequence of the DNA-condensing polypeptide protamine (PN), singly or as a pair: LLO-PN and LLO-PNPN. We demonstrate dramatic enhancement of the gene delivery efficiency of protamine-condensed DNA upon incorporation of a small amount of LLO-PN fusion protein and further improvement with LLO-PNPN in vitro using cultured cells. Additionally, the association of anionic liposomes with cationic LLO-PNPN/protamine/DNA complexes, yielding a net negative surface charge, resulted in better in vitro transfection efficiency in the presence of serum. An initial, small set of data in mice indicated that the observed enhancement in gene expression could also be applicable to in vivo gene delivery. This study suggests that incorporation of a recombinant fusion protein with multiple functional components, such as LLO-protamine fusion protein, in a nonviral vector is a promising strategy for various nonviral gene delivery systems.
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