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      Platform technologies for modern vaccine manufacturing

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      Author(s): , *
      Publication date (Electronic):
      Journal: Vaccine
      Publisher: Elsevier Ltd.
      Keywords: Virus-like particle, Liposome, Vaccine design, Modular, Platform technology

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          Abstract

          Improved understanding of antigenic components and their interaction with the immune system, as supported by computational tools, permits a sophisticated approach to modern vaccine design. Vaccine platforms provide an effective tool by which strategically designed peptide and protein antigens are modularized to enhance their immunogenicity. These modular vaccine platforms can overcome issues faced by traditional vaccine manufacturing and have the potential to generate safe vaccines, rapidly and at a low cost. This review introduces two promising platforms based on virus-like particle and liposome, and discusses the methodologies and challenges.

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          Virus-like particles as a highly efficient vaccine platform: Diversity of targets and production systems and advances in clinical development

          Natasha Kushnir, Stephen Streatfield, Vidadi Yusibov (2012)
          Highlights ► Virus-like particles (VLPs) are a class of recombinant subunit vaccines. ► VLPs resemble native viruses but lack infectious genetic material. ► VLPs are promising vaccines due to strong immunogenicity and safety. ► VLPs can be produced in prokaryotic or eukaryotic expression systems, or in vitro. ► VLP-based vaccine candidates targeting many diseases are in clinical development.
          Article 0 comments Cited 195 times – based on 0 reviews     Review now
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            Influenza A vaccine based on the extracellular domain of M2: weak protection mediated via antibody-dependent NK cell activity.

            Alina Bachmann, Tazio Storni, Andrea Jegerlehner … (2004)
            Vaccination of mice with a peptide corresponding to the extracellular part of M2 protein coupled to the immunodominant domain of hepatitis B core can protect mice from a lethal challenge with influenza A virus. As the extracellular part of M2 protein is highly conserved in all known human influenza A strains, such a vaccine may protect against all human influenza A strains, which would represent a major advantage over current vaccine strategies. The present study demonstrates that protection is mediated exclusively by Abs, a very important feature of a successful preventive vaccine. However, these Abs neither bind efficiently to the free virus nor neutralize virus infection, but bind to M2 protein expressed on the surface of virus-infected cells. The presence of NK cells is important for protection, whereas complement is not, supposing that protection is mediated via Ab-dependent, cell-mediated cytotoxicity. The absence of neutralizing Abs results in much weaker protection than that achieved by vaccination with UV-inactivated influenza virus. Specifically, whereas neutralizing Abs completely eliminate signs of disease even at high viral challenge doses, M2-specific Abs cannot prevent infection, but merely reduce disease at low challenge doses. M2-specific Abs fail to protect from high challenge doses, as vaccinated mice undergo lethal infection under these conditions. In conclusion, protection mediated by M2-hepatitis B core vaccine would be insufficient during the yearly epidemics, for which full protection is desirable, and overall is clearly inferior to protection achieved by immunization with classical inactivated viral preparations.
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              Bioengineering virus-like particles as vaccines.

              Frank Sainsbury, Natalie K. Connors, Nani Wibowo … (2014)
              Virus-like particle (VLP) technology seeks to harness the optimally tuned immunostimulatory properties of natural viruses while omitting the infectious trait. VLPs that assemble from a single protein have been shown to be safe and highly efficacious in humans, and highly profitable. VLPs emerging from basic research possess varying levels of complexity and comprise single or multiple proteins, with or without a lipid membrane. Complex VLP assembly is traditionally orchestrated within cells using black-box approaches, which are appropriate when knowledge and control over assembly are limited. Recovery challenges including those of adherent and intracellular contaminants must then be addressed. Recent commercial VLPs variously incorporate steps that include VLP in vitro assembly to address these problems robustly, but at the expense of process complexity. Increasing research activity and translation opportunity necessitate bioengineering advances and new bioprocessing modalities for efficient and cost-effective production of VLPs. Emerging approaches are necessarily multi-scale and multi-disciplinary, encompassing diverse fields from computational design of molecules to new macro-scale purification materials. In this review, we highlight historical and emerging VLP vaccine approaches. We overview approaches that seek to specifically engineer a desirable immune response through modular VLP design, and those that seek to improve bioprocess efficiency through inhibition of intracellular assembly to allow optimal use of existing purification technologies prior to cell-free VLP assembly. Greater understanding of VLP assembly and increased interdisciplinary activity will see enormous progress in VLP technology over the coming decade, driven by clear translational opportunity. © 2013 Wiley Periodicals, Inc.
              Article 0 comments Cited 115 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Linda H.L. Lua
                Journal
                Journal ID (nlm-ta): Vaccine
                Journal ID (iso-abbrev): Vaccine
                Title: Vaccine
                Publisher: Elsevier Ltd.
                ISSN (Print): 0264-410X
                ISSN (Electronic): 1873-2518
                Publication date PMC-release: 25 March 2017
                Publication date (Print): 16 August 2017
                Publication date (Electronic): 25 March 2017
                Volume: 35
                Issue: 35
                Pages: 4480-4485
                Affiliations
                The University of Queensland, Protein Expression Facility, St Lucia, QLD 4072, Australia
                Author notes
                [* ]Corresponding author. l.lua@ 123456uq.edu.au
                Article
                Publisher ID: S0264-410X(17)30365-1
                DOI: 10.1016/j.vaccine.2017.02.069
                PMC ID: 7115529
                PubMed ID: 28347504
                SO-VID: d5a5b0f2-d6ef-4dbd-bc71-83c4590f22e8
                Copyright © © 2017 Elsevier Ltd. All rights reserved.
                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.

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                Subject: Article

                ScienceOpen disciplines: Infectious disease & Microbiology
                Keywords: virus-like particle,liposome,vaccine design,modular,platform technology
                Data availability:
                ScienceOpen disciplines: Infectious disease & Microbiology
                Keywords: virus-like particle, liposome, vaccine design, modular, platform technology

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