Encapsulins-Bacterial Protein Nanocompartments: Structure, Properties, and Application - PubMed (original) (raw)

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Encapsulins-Bacterial Protein Nanocompartments: Structure, Properties, and Application

Anna N Gabashvili et al. Biomolecules. 2020.

Abstract

Recently, a new class of prokaryotic compartments, collectively called encapsulins or protein nanocompartments, has been discovered. The shell proteins of these structures self-organize to form icosahedral compartments with a diameter of 25-42 nm, while one or more cargo proteins with various functions can be encapsulated in the nanocompartment. Non-native cargo proteins can be loaded into nanocompartments and the surface of the shells can be further functionalized, which allows for developing targeted drug delivery systems or using encapsulins as contrast agents for magnetic resonance imaging. Since the genes encoding encapsulins can be integrated into the cell genome, encapsulins are attractive for investigation in various scientific fields, including biomedicine and nanotechnology.

Keywords: MRI; cell labeling; encapsulin; nanocompartment.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1

Figure 1

Structural comparison of the capsomers/monomers and assembled capsid/encapsulins: (A) HK97 phage, (B) Thermotoga maritima encapsulin, (C) Myxococcus xanthus encapsulin, (D) Pyrococcus furiosus encapsulin. (PDB-ID: 2FT1, 3DKT, 4PT2, and 2E0Z, respectively).

Figure 2

Figure 2

The cargo loading peptide coding sequence can be located at either the 5′ or 3′ end of the cargo loading peptide gene (A,B) with formation of the encapsulin structure (D). In some cases, the cargo protein encoding gene and encapsulin shell encoding gene are fused (C), and there is no need for a cargo-loading peptide to form encapsulin structure (E).

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References

    1. Valdes-Stauber N., Scherer S. Isolation and Characterization of Linocin M18, a Bacteriocin Produced by Brevibacterium Linens. Appl. Environ. Microbiol. 1994;60:3809–3814. doi: 10.1128/AEM.60.10.3809-3814.1994. - DOI - PMC - PubMed
    1. Sutter M., Boehringer D., Gutmann S., Günther S., Prangishvili D., Loessner M.J., Stetter K.O., Weber-Ban E., Ban N. Structural Basis of Enzyme Encapsulation into a Bacterial Nanocompartment. Nat. Struct. Mol. Biol. 2008;15:939–947. doi: 10.1038/nsmb.1473. - DOI - PubMed
    1. Giessen T.W. Encapsulins: Microbial Nanocompartments with Applications in Biomedicine, Nanobiotechnology and Materials Science. Curr. Opin. Chem. Biol. 2016;34:1–10. doi: 10.1016/j.cbpa.2016.05.013. - DOI - PubMed
    1. Rosenkrands I., Rasmussen P.B., Carnio M., Jacobsen S., Theisen M., Andersen P. Identification and Characterization of a 29-Kilodalton Protein from Mycobacterium Tuberculosis Culture Filtrate Recognized by Mouse Memory Effector Cells. Infect. Immun. 1998;66:2728–2735. doi: 10.1128/IAI.66.6.2728-2735.1998. - DOI - PMC - PubMed
    1. Hicks P.M., Rinker K.D., Baker J.R., Kelly R.M. Homomultimeric Protease in the Hyperthermophilic Bacterium Thermotoga Maritima Has Structural and Amino Acid Sequence Homology to Bacteriocins in Mesophilic Bacteria. FEBS Lett. 1998;440:393–398. doi: 10.1016/S0014-5793(98)01451-3. - DOI - PubMed

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