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The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design

Protein assemblies provide unique structural features which make them useful as carrier molecules in biomedical and chemical science. Protein assemblies can accommodate a variety of organic, inorganic and biological molecules such as small proteins and peptides and have been used in development of s...

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Detalles Bibliográficos
Autores principales: Nguyen, Que Dan, Kikuchi, Kosuke, Maity, Basudev, Ueno, Takafumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7919822/
https://www.ncbi.nlm.nih.gov/pubmed/33669238
http://dx.doi.org/10.3390/ijms22041934
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author Nguyen, Que Dan
Kikuchi, Kosuke
Maity, Basudev
Ueno, Takafumi
author_facet Nguyen, Que Dan
Kikuchi, Kosuke
Maity, Basudev
Ueno, Takafumi
author_sort Nguyen, Que Dan
collection PubMed
description Protein assemblies provide unique structural features which make them useful as carrier molecules in biomedical and chemical science. Protein assemblies can accommodate a variety of organic, inorganic and biological molecules such as small proteins and peptides and have been used in development of subunit vaccines via display parts of viral pathogens or antigens. Such subunit vaccines are much safer than traditional vaccines based on inactivated pathogens which are more likely to produce side-effects. Therefore, to tackle a pandemic and rapidly produce safer and more effective subunit vaccines based on protein assemblies, it is necessary to understand the basic structural features which drive protein self-assembly and functionalization of portions of pathogens. This review highlights recent developments and future perspectives in production of non-viral protein assemblies with essential structural features of subunit vaccines.
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spelling pubmed-79198222021-03-02 The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design Nguyen, Que Dan Kikuchi, Kosuke Maity, Basudev Ueno, Takafumi Int J Mol Sci Review Protein assemblies provide unique structural features which make them useful as carrier molecules in biomedical and chemical science. Protein assemblies can accommodate a variety of organic, inorganic and biological molecules such as small proteins and peptides and have been used in development of subunit vaccines via display parts of viral pathogens or antigens. Such subunit vaccines are much safer than traditional vaccines based on inactivated pathogens which are more likely to produce side-effects. Therefore, to tackle a pandemic and rapidly produce safer and more effective subunit vaccines based on protein assemblies, it is necessary to understand the basic structural features which drive protein self-assembly and functionalization of portions of pathogens. This review highlights recent developments and future perspectives in production of non-viral protein assemblies with essential structural features of subunit vaccines. MDPI 2021-02-16 /pmc/articles/PMC7919822/ /pubmed/33669238 http://dx.doi.org/10.3390/ijms22041934 Text en © 2021 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
Nguyen, Que Dan
Kikuchi, Kosuke
Maity, Basudev
Ueno, Takafumi
The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design
title The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design
title_full The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design
title_fullStr The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design
title_full_unstemmed The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design
title_short The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design
title_sort versatile manipulations of self-assembled proteins in vaccine design
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7919822/
https://www.ncbi.nlm.nih.gov/pubmed/33669238
http://dx.doi.org/10.3390/ijms22041934
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