Fabrication of uniform layer-by-layer assemblies with complementary protein cage nanobuilding blocks via simple His-tag/metal recognition

Moon, Hyojin; Kim, Woo Gyum; Lim, Seongdong; Kang, Young Ji; Shin, Hong Ju; Ko, Hyunhyub; Hong, Sung You; Kang, Sebyung

doi:10.1039/c3tb20554a

Cited by 21 publications

(34 citation statements)

References 41 publications

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“…We started with a genetically modified encapsulin, which has only one cysteine per subunit at position 123. Cell targeting peptide with linker (GGGGGGDCAWHLGELVWCTGGGGG) was inserted into residues between 138 and 139 of encapsulin by an established polymerase chain reaction (PCR) protocol using pET-30b based plasmids containing genes encoding encapsulin [ 20 ].…”

Section: Methodsmentioning

confidence: 99%

“…The suspension was sonicated for 10 min in 30 s intervals, and subsequently centrifuged at 12000 g for 1 hr at 4°C. Encapsulin protein cage was purified by size exclusion chromatography (SEC) after heat precipitation for 10 min at 65°C [ 20 ].…”

Section: Methodsmentioning

confidence: 99%

“…The molecular masses of each species can be determined from the charges and the observed mass-to-charge (m/z) ratio values. Mass spectra were acquired in the range of m/z 500-3000 and deconvoluted using MaxEnt1 from MassLynx version 4.1 to obtain the average mass from multiple charge state distributions [ 20 ].…”

Section: Methodsmentioning

confidence: 99%

“…Protein cages, such as ferritins [ 12 , 16 – 19 ], viral capsids [ 17 , 20 – 24 ], lumazine synthase [ 20 , 25 , 26 ], and encapsulin [ 27 ], are promising nanoplatform candidates for efficient delivery systems of diagnostics and/or therapeutics because they have uniform size and structure as well as high biocompatibility and biodegradability [ 1 ]. Protein cages are spontaneously self-assembled from multiple copies of one or a few types of protein subunits in a precisely controlled manner.…”

Section: Introductionmentioning

confidence: 99%

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Genetically engineering encapsulin protein cage nanoparticle as a SCC-7 cell targeting optical nanoprobe

et al. 2014

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BackgroundProtein cage nanoparticles are promising nanoplatform candidates for efficient delivery systems of diagnostics and/or therapeutics because of their uniform size and structure as well as high biocompatibility and biodegradability. Encapsulin protein cage nanoparticle is used to develop a cell-specific targeting optical nanoprobe.ResultsFcBPs are genetically inserted and successfully displayed on the surface of encapsulin to form FcBP-encapsulin. Selectively binding of FcBP-encapsulin to SCC-7 is visualized with fluorescent microscopy.ConclusionsEncapsulin protein cage nanoparticle is robust enough to maintain their structure at high temperature and easily acquires multifunctions on demand through the combination of genetic and chemical modifications.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Genetically engineering encapsulin protein cage nanoparticle as a SCC-7 cell targeting optical nanoprobe

et al. 2014

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“…Samples were loaded onto the MassPREP Micro desalting column (Waters) and eluted with a gradient of 5-95% (v/v) acetonitrile containing 0.1% formic acid with a flow rate of 300 µL/min [11]. Mass spectra were acquired in the range of m/z 500-3,000 and processed using MaxEnt 1 and MaxEnt 3 from MassLynx version 4.1 to obtain the average mass from multiple charge state distributions.…”

Section: Methodsmentioning

confidence: 99%

Lumazine synthase protein cage nanoparticles as antigen delivery nanoplatforms for dendritic cell-based vaccine development

Shin

Kang

et al. 2014

Clin Exp Vaccine Res

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PurposeProtein cages are promising nanoplatform candidates for efficient delivery systems due to their homogenous size and structure with high biocompatibility and biodegradability. In this study, we investigate the potential of lumazine synthase protein cage as an antigen delivery system to dendritic cells (DCs), which induce antigen-specific T cell proliferation.Materials and MethodsOvalbumin (OVA) peptides OT-1 (SIINFEKL) and OT-2 (ISQAVHAAHAEINEAGR) were genetically inserted to lumazine synthase and each protein cage was over-expressed in Escherichia coli as a soluble protein. The efficiency of antigen delivery and the resulting antigen-specific T cell proliferation by DCs was examined in vitro as well as in vivo.ResultsWe successfully generated and characterized OVA peptides carrying lumazine synthase protein cages. The OT-1 and OT-2 peptides carried by lumazine synthases were efficiently delivered and processed by DCs in vitro as well as in vivo, and induced proliferation of OT-1-specific CD8+T cells and OT-2-specific CD4+T cells.ConclusionOur data demonstrate the potential of lumazine synthase protein cage being used as a novel antigen delivery system for DC-based vaccine development in future clinical applications.

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Selective and Effective Cancer Treatments using Target‐Switchable Intracellular Bacterial Toxin Delivery Systems

Park

Choi

Bae

et al. 2020

Advanced Therapeutics

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Targeted cancer therapies have been extensively tested with the purpose to selectively suppress tumor growth and to avoid harming healthy tissue. However, failure to escape endosomes upon receptor‐mediated endocytosis is a major obstacle limiting the efficacy of targeted cancer therapeutics. Here, novel target‐switchable intracellular toxin delivery systems (TiTDS) are presented which use the catalytic and translocation domain of diphtheria toxin (dtA‐T) as an intracellular toxin delivery platform and affibody molecules targeting human epidermal growth factor receptor 2 or epidermal growth factor receptor (HER2Afb or EGFRAfb) as target‐specific ligands. The intracellular toxin delivery platform and the affibody molecules are genetically fused with SpyCatcher (SC) protein and SpyTag (ST) peptide, respectively, to generate dtA‐T‐SC and ST‐HER2Afb or ST‐EGFRAfb modules. These modules can be individually purified and post‐translationally ligated to produce dtA‐T/HER2Afb or dtA‐T/EGFRAf. dtA‐T/HER2Afb and dtA‐T/EGFRAfb can selectively bind to their corresponding target cancer cells, efficiently enter the cells through receptor‐mediated endocytosis, successfully escape endosomes, and release toxins into the cytosol. They exhibit high target‐specific cytotoxicity in vitro and can significantly reduce tumor masses in vivo. TiTDS is a promising targeted cancer therapy platform because of its high target specificity, effective intracellular delivery of active toxins with improved therapeutic efficacy, and target switchability.

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Fabrication of uniform layer-by-layer assemblies with complementary protein cage nanobuilding blocks via simple His-tag/metal recognition

Cited by 21 publications

References 41 publications

Genetically engineering encapsulin protein cage nanoparticle as a SCC-7 cell targeting optical nanoprobe

Genetically engineering encapsulin protein cage nanoparticle as a SCC-7 cell targeting optical nanoprobe

Lumazine synthase protein cage nanoparticles as antigen delivery nanoplatforms for dendritic cell-based vaccine development

Selective and Effective Cancer Treatments using Target‐Switchable Intracellular Bacterial Toxin Delivery Systems

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