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Open AccessJournal ArticleDOI

Nanotechnological Applications Based on Bacterial Encapsulins

TLDR
Encapsulins are proteinaceous nanocontainers, constructed by a single species of shell protein that self-assemble into 20-40 nm icosahedral particles as mentioned in this paper.
Abstract
Encapsulins are proteinaceous nanocontainers, constructed by a single species of shell protein that self-assemble into 20-40 nm icosahedral particles. Encapsulins are structurally similar to the capsids of viruses of the HK97-like lineage, to which they are evolutionarily related. Nearly all these nanocontainers encase a single oligomeric protein that defines the physiological role of the complex, although a few encapsulate several activities within a single particle. Encapsulins are abundant in bacteria and archaea, in which they participate in regulation of oxidative stress, detoxification, and homeostasis of key chemical elements. These nanocontainers are physically robust, contain numerous pores that permit metabolite flux through the shell, and are very tolerant of genetic manipulation. There are natural mechanisms for efficient functionalization of the outer and inner shell surfaces, and for the in vivo and in vitro internalization of heterologous proteins. These characteristics render encapsulin an excellent platform for the development of biotechnological applications. Here we provide an overview of current knowledge of encapsulin systems, summarize the remarkable toolbox developed by researchers in this field, and discuss recent advances in the biomedical and bioengineering applications of encapsulins.

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Citations
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Encapsulins from Ca. Brocadia fulgida: An effective tool to enhance the tolerance of engineered bacteria (pET-28a-cEnc) to Zn2.

TL;DR: Zhang et al. as discussed by the authors used tandem mass tag-based quantitative proteomic analysis to reveal the underlying regulatory mechanism by which the genetically-engineered bacteria (with cEnc) adapted to Zn2+ stress.
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Recent advances in the structural biology of encapsulin bacterial nanocompartments

TL;DR: In this paper , the authors summarize findings from recent encapsulin structures that have significant implications for their biological roles and compare important features such as the E-loop, cargo-peptide binding site, and fivefold axis channel in different structures.
Journal ArticleDOI

A Dual-Metal-Catalyzed Sequential Cascade Reaction in an Engineered Protein Cage.

TL;DR: In this paper , the authors describe the creation of an artificial protein cage housing a dual metal-tagged guest protein that catalyzes a linear, two-step sequential cascade reaction, consisting of a fusion protein of HaloTag and monomeric rhizavidin.
Journal ArticleDOI

Encapsulin cargo loading: progress and potential.

TL;DR: Encapsulins are a recently discovered class of prokaryotic self-assembling icosahedral protein nanocompartments measuring between 24 and 42 nm in diameter, capable of selectively encapsulating dedicated cargo proteins in vivo as discussed by the authors .
Journal ArticleDOI

A Dual‐Metal‐Catalyzed Sequential Cascade Reaction in an Engineered Protein Cage**

TL;DR: In this article , the authors describe the creation of an artificial protein cage housing a dual-metal-tagged guest protein that catalyzes a linear, two-step sequential cascade reaction.
References
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