Design of Enzyme‐Encapsulated Protein Containers by In Vivo Crystal Engineering

Abe, Satoshi; Ijiri, Hiroshi; Negishi, Hashiru; Yamanaka, Hiroyuki; Sasaki, K.; Hirata, Kunio; Mori, Hajime; Ueno, Takafumi

doi:10.1002/adma.201503827

Cited by 32 publications

(40 citation statements)

References 27 publications

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“…19). 128 The crystal structure of WTPhCs indicates that the side chain of Arg13 at the tip of the H1-helix is expected to contribute to the robust character of the crystals by the formation of intermolecular hydrogen bonds. Two mutant crystals were designed, in which Arg13 is replaced with Ala and Lys, R13APhMs and R13KPhMs, respectively.…”

Section: In Vivo Crystal Engineeringmentioning

confidence: 99%

Design of a confined environment using protein cages and crystals for the development of biohybrid materials

2016

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There is growing interest in the design of protein assemblies for use in materials science and bionanotechnology. Protein assemblies, such as cages and crystalline protein structures, provide confined chemical environments that allow immobilization of metal complexes, nanomaterials, and proteins by metal coordination, assembly/disassembly reactions, genetic manipulation and crystallization methods. Protein assembly composites can be used to prepare hybrid materials with catalytic, magnetic and optical properties for cellular applications due to their high stability, solubility and biocompatibility. In this feature article, we focus on the recent development of ferritin as the most promising molecular template protein cage and in vivo and in vitro engineering of protein crystals as solid protein materials with functional properties.

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Section: In Vivo Crystal Engineeringmentioning

confidence: 99%

Design of a confined environment using protein cages and crystals for the development of biohybrid materials

2016

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“…Because of the wide range of programmable intermolecular interactions available, protein-based molecular frameworks can be finely tuned to control their properties. Although less prevalent that MOFs, examples of protein-based molecular frameworks are emerging and include protein crystals that have been created not for structure elucidation but as a scaffold to selectively confine and store enzymes as well as crystalline protein assemblies, which exhibit controlled porosity. , Here we describe the formation of a protein macromolecular framework (PMF), which is conceptually analogous to a MOF but is composed only of protein cages, derived from a virus, and protein linkers.…”

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confidence: 99%

Templated Assembly of a Functional Ordered Protein Macromolecular Framework from P22 Virus-like Particles

et al. 2018

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Bottom-up construction of mesoscale materials using biologically derived nanoscale building blocks enables engineering of desired physical properties using green production methods. Virus-like particles (VLPs) are exceptional building blocks due to their monodispersed sizes, geometric shapes, production ease, proteinaceous composition, and our ability to independently functionalize the interior and exterior interfaces. Here a VLP, derived from bacteriophage P22, is used as a building block for the fabrication of a protein macromolecular framework (PMF), a tightly linked 3D network of functional protein cages that exhibit long-range order and catalytic activity. Assembly of PMFs was electrostatically templated, using amine-terminated dendrimers, then locked into place with a ditopic cementing protein that binds to P22. Long-range order is preserved on removal of the dendrimer, leaving a framework material composed completely of protein. Encapsulation of β-glucosidase enzymes inside of P22 VLPs results in formation of stable, condensed-phase materials with high local concentration of enzymes generating catalytically active PMFs.

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“…However, the RPS of immunized fish with polyhedra incorporating H1-D4ORF and D4ORF-VP3 proteins was lower compared with previous reports. The different efficacy of these vaccines may be related to the slow release of antigens em-bedded in the polyhedra under physiological conditions [20,22], different types of vac-cines, different routes of administration and different detection time.…”

Section: Discussionmentioning

confidence: 99%

“…These results indicated that vaccine carriers and the effective release of vaccine proteins from their carriers are crucial for oral vaccines. Although polyhedra are very stable, encapsulated protein kinase C [20], fibroblast growth factor (FGF)-2 [17,21,22], FGF-7 [17,22], epidermal growth factor [17,22], leukemia inhibitory factor [23], bone morphogenetic protein-2 [24], vascular endothelial growth factor [19], endostatin [19], and the major capsid protein VP1 of norovirus [18] were reported to be released from polyhedra both in vitro and in vivo.…”

Section: Discussionmentioning

confidence: 99%

“…The atomic structure of BmCPVpolyhedra showed that the polyhedrin H1-helix (the H1 tag, with 30 amino acid residues at the N-terminus) of the molecule is a useful tag for incorporating recombinant proteins into polyhedra such as the VP3 immobilization signal [17]. Thus far, the major capsid protein VP1 of norovirus-like particles [18], vascular endothelial growth factor [19], endostatin [19], protein kinase C [20], fibroblast growth factors [21,22], leukemia inhibitory factor [23], and bone morphogenetic protein-2 [24] have beenincorporated into polyhedra by co-expression of BmCPVpolyhedrin and the target gene fused with the H1 tag or the VP3 tag. However, until now, there have been no reports on the incorporation of recombinant vaccines into BmCPVpolyhedra or an evaluation of the immune-protective effects of apolyhedron-incorporating vaccine.…”

Section: Introductionmentioning

confidence: 99%

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Incidence of Carassius auratus Gibelio Gill Hemorrhagic Disease Caused by CyHV-2 Infection Can Be Reduced by Vaccination with Polyhedra Incorporating Antigens

Zhang

Liu

et al. 2021

Vaccines

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Encapsulation of antigens within protein microcrystals (polyhedra) is a promising approach for the stable delivery of vaccines. In this study, a vaccine was encapsulated into polyhedra against cyprinid herpesvirus II (CyHV-2). CyHV-2 typically infects gibel carp, Carassius auratus gibelio, causing gill hemorrhagic disease. The vaccine was constructed using a codon-optimized sequence, D4ORF, comprising the ORF72 (region 1–186 nt), ORF66 (region 993–1197 nt), ORF81 (region 603–783 nt), and ORF82 (region 85–186 nt) genes of CyHV-2. The H1-D4ORF and D4ORF-VP3 sequences were, respectively, obtained by fusing the H1-helix sequence (region 1–90 nt) ofBombyx mori cypovirus(BmCPV) polyhedrin to the 5′ terminal end of D4ORF and by fusing a partial sequence (1–279 nt) of the BmCPV VP3 gene to the 3′ terminal end of D4ORF. Furthermore, BmNPV-H1-D4ORF-polh and BmNPV-D4ORF-VP3-polh recombinant B. mori nucleopolyhedroviruses (BmNPVs), belonging to the family Baculoviridae, and co-expressing BmCPV polyhedrin and H1-D4ORF or D4ORF-VP3, were constructed. H1-D4ORF and D4ORF-VP3 fusion proteins were confirmed to be encapsulated into recombinant cytoplasmic polyhedra by Western blotting. Degradation of vaccine proteins was assessed by SDS-PAGE, and the results showed that the encapsulated vaccine proteins in polyhedra could be protected from degradation. Furthermore, when gibel carp were vaccinated with the purified polyhedra from BmNPV-H1-D4ORF-polh and BmNPV-D4ORF-VP3-polh via injection, the antibody titers in the serum of the vaccinated fish reached 1:6400–1:12,800 at 3 weeks post-vaccination. Therelative percentage of survival of immunized gibel carp reached 64.71% and 58.82%, respectively, following challenge with CyHV-2. These results suggest that incorporating vaccine protein into BmCPV polyhedra may be a novel approach for developing aquaculture microencapsulated vaccines.

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Design of Enzyme‐Encapsulated Protein Containers by In Vivo Crystal Engineering

Cited by 32 publications

References 27 publications

Design of a confined environment using protein cages and crystals for the development of biohybrid materials

Design of a confined environment using protein cages and crystals for the development of biohybrid materials

Templated Assembly of a Functional Ordered Protein Macromolecular Framework from P22 Virus-like Particles

Incidence of Carassius auratus Gibelio Gill Hemorrhagic Disease Caused by CyHV-2 Infection Can Be Reduced by Vaccination with Polyhedra Incorporating Antigens

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