REVIEW ARTICLE
Assessment of Different Expression Strategies for the Production of a Recombinant Lipoprotein Vaccine in Plants
Anna Hennig1, 2, Yvonne Reinders2, Anatoli Giritch3, Jörg Reinders2, Heribert Warzecha1, 2, *
Article Information
Identifiers and Pagination:
Year: 2008Volume: 2
First Page: 51
Last Page: 55
Publisher ID: TOBIOTJ-2-51
DOI: 10.2174/1874070700802010051
Article History:
Received Date: 07/11/2007Revision Received Date: 21/12/2007
Acceptance Date: 21/12/2007
Electronic publication date: 6/2/2008
Collection year: 2008
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: (https://creativecommons.org/licenses/by/4.0/legalcode). This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
The ability of plants to serve as a production system for bacterial lipoprotein vaccines has been investigated. First, the effect of high-level expression of the Borrelia burgdorferi outer membrane protein A (OspA), a prototype vaccine against Lyme disease, has been examined by a proteomics approach. Analysis by 2D-PAGE of wild type tobacco plants and transplastomic plants accumulating recombinant OspA showed no apparent differences in protein pattern except for OspA. However, presence of the bacterial signal sequence limits transgene accumulation. As an alternative approach OspA was produced in Nicotiana benthamiana plants by transient expression via a deconstructed tobacco mosaic virus-based system. While rapid expression of OspA could be achieved, no palmitoylation occurred with the genuine bacterial sequence. In contrast, modification of the N-terminus with an eukaryotic sequence motif resulted in palmitoylation of OspA. This study shows that plants provide multiple expression strategies and could serve as a versatile production platform for recombinant lipidated subunit vaccines.
