Virus-like particles: the future of microbial factories and cell-free systems as platforms for vaccine development

There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

Abstract

Highlights

▶ Microorganisms are inexpensive platforms to produce chimeric VLPs. ▶ Bacteriophage-derived VLPs are excellent structures for drug delivery. ▶ Microbial cell factories offer versatility and scalability for VLP production. ▶ Cell-free systems are technologies with potential but more development is needed. ▶ Neglected diseases will be treated with VLP technologies with profitable margin.

Abstract

Vaccines based on virus-like particles have proved their success in human health. More than 25 years after the approval of the first vaccine based on this technology, the substantial efforts to expand the range of applications and target diseases are beginning to bear fruit. The incursion of high-throughput screening technologies, combined with new developments in protein engineering and chemical coupling, have accelerated the development of systems capable of producing macrostructures useful for vaccinology, gene delivery, immunotherapy and bionanotechnology. This review summarizes the most recent developments in microbial cell factories and cell-free systems for virus-like particle production and discusses the future impact of this technology in human and animal health.

Related collections

Most cited references 43

Record: found
Abstract: found
Article: not found

Cell-free protein synthesis: applications come of age.

Erik Carlson, Rui Gan, C Hodgman … (2012)

Cell-free protein synthesis has emerged as a powerful technology platform to help satisfy the growing demand for simple and efficient protein production. While used for decades as a foundational research tool for understanding transcription and translation, recent advances have made possible cost-effective microscale to manufacturing scale synthesis of complex proteins. Protein yields exceed grams protein produced per liter reaction volume, batch reactions last for multiple hours, costs have been reduced orders of magnitude, and reaction scale has reached the 100-liter milestone. These advances have inspired new applications in the synthesis of protein libraries for functional genomics and structural biology, the production of personalized medicines, and the expression of virus-like particles, among others. In the coming years, cell-free protein synthesis promises new industrial processes where short protein production timelines are crucial as well as innovative approaches to a wide range of applications. Copyright © 2011 Elsevier Inc. All rights reserved.

0 comments Cited 179 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: not found
Article: not found

Biopharmaceutical benchmarks 2010.

Gary Walsh (2010)

0 comments Cited 160 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: found
Article: found

Is Open Access

Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli

Van Dat Nguyen, Feras Hatahet, Kirsi Salo … (2011)

Background Disulfide bonds are one of the most common post-translational modifications found in proteins. The production of proteins that contain native disulfide bonds is challenging, especially on a large scale. Either the protein needs to be targeted to the endoplasmic reticulum in eukaryotes or to the prokaryotic periplasm. These compartments that are specialised for disulfide bond formation have an active catalyst for their formation, along with catalysts for isomerization to the native state. We have recently shown that it is possible to produce large amounts of prokaryotic disulfide bond containing proteins in the cytoplasm of wild-type bacteria such as E. coli by the introduction of catalysts for both of these processes. Results Here we show that the introduction of Erv1p, a sulfhydryl oxidase and a disulfide isomerase allows the efficient formation of natively folded eukaryotic proteins with multiple disulfide bonds in the cytoplasm of E. coli. The production of disulfide bonded proteins was also aided by the use of an appropriate fusion protein to keep the folding intermediates soluble and by choice of media. By combining the pre-expression of a sulfhydryl oxidase and a disulfide isomerase with these other factors, high level expression of even complex disulfide bonded eukaryotic proteins is possible Conclusions Our results show that the production of eukaryotic proteins with multiple disulfide bonds in the cytoplasm of E. coli is possible. The required exogenous components can be put onto a single plasmid vector allowing facile transfer between different prokaryotic strains. These results open up new avenues for the use of E. coli as a microbial cell factory.

0 comments Cited 126 times – based on 0 reviews      Review now

Bookmark

All references

Author and article information

Contributors

Keith EJ Tyo

Journal

Journal ID (nlm-ta): Curr Opin Biotechnol

Journal ID (iso-abbrev): Curr. Opin. Biotechnol

Title: Current Opinion in Biotechnology

Publisher: Elsevier Ltd.

ISSN (Print): 0958-1669

ISSN (Electronic): 1879-0429

Publication date PMC-release: 4 March 2013

Publication date (Print): December 2013

Publication date (Electronic): 4 March 2013

Volume: 24

Issue: 6

Pages: 1089-1093

Affiliations

[0005]Department of Chemical and Biological Engineering, Northwestern University, 2145 Sheridan Road, Evanston, IL 60208, United States

Article

Publisher ID: S0958-1669(13)00022-0

DOI: 10.1016/j.copbio.2013.02.008

PMC ID: 7127385

PubMed ID: 23481378

SO-VID: 9e22048f-48c0-4db6-81c5-70b0bec8b08e

License:

Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

Virus-like particles: the future of microbial factories and cell-free systems as platforms for vaccine development

Read this article at

Abstract

Highlights

Abstract

Related collections

Genome Engineering using CRISPR

Most cited references 43

Cell-free protein synthesis: applications come of age.

Biopharmaceutical benchmarks 2010.

Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli

Author and article information

Contributors

Journal

Affiliations

Article

History

Categories

Comments

Comment on this article

Similar content 1,045

Cited by 37

Most referenced authors 1,245