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

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 functi...

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Autores principales: Gabashvili, Anna N., Chmelyuk, Nelly S., Efremova, Maria V., Malinovskaya, Julia A., Semkina, Alevtina S., Abakumov, Maxim A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7355545/
https://www.ncbi.nlm.nih.gov/pubmed/32604934
http://dx.doi.org/10.3390/biom10060966
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author Gabashvili, Anna N.
Chmelyuk, Nelly S.
Efremova, Maria V.
Malinovskaya, Julia A.
Semkina, Alevtina S.
Abakumov, Maxim A.
author_facet Gabashvili, Anna N.
Chmelyuk, Nelly S.
Efremova, Maria V.
Malinovskaya, Julia A.
Semkina, Alevtina S.
Abakumov, Maxim A.
author_sort Gabashvili, Anna N.
collection PubMed
description 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.
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spelling pubmed-73555452020-07-23 Encapsulins—Bacterial Protein Nanocompartments: Structure, Properties, and Application Gabashvili, Anna N. Chmelyuk, Nelly S. Efremova, Maria V. Malinovskaya, Julia A. Semkina, Alevtina S. Abakumov, Maxim A. Biomolecules Review 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. MDPI 2020-06-26 /pmc/articles/PMC7355545/ /pubmed/32604934 http://dx.doi.org/10.3390/biom10060966 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Gabashvili, Anna N.
Chmelyuk, Nelly S.
Efremova, Maria V.
Malinovskaya, Julia A.
Semkina, Alevtina S.
Abakumov, Maxim A.
Encapsulins—Bacterial Protein Nanocompartments: Structure, Properties, and Application
title Encapsulins—Bacterial Protein Nanocompartments: Structure, Properties, and Application
title_full Encapsulins—Bacterial Protein Nanocompartments: Structure, Properties, and Application
title_fullStr Encapsulins—Bacterial Protein Nanocompartments: Structure, Properties, and Application
title_full_unstemmed Encapsulins—Bacterial Protein Nanocompartments: Structure, Properties, and Application
title_short Encapsulins—Bacterial Protein Nanocompartments: Structure, Properties, and Application
title_sort encapsulins—bacterial protein nanocompartments: structure, properties, and application
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7355545/
https://www.ncbi.nlm.nih.gov/pubmed/32604934
http://dx.doi.org/10.3390/biom10060966
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