Foliar extracts from transgenic tomato plants expressing the structural polyprotein, P1-2A, and protease, 3C, from foot-and-mouth disease virus elicit a protective response in guinea pigs

Pan, Li; Zhang, Yongguang; Wang, Yonglu; Wang, Baoqin; Wang, Wenxiu; Fang, Yuqi; Jiang, Shoutian; Lv, Jing; Wang, Wei; Sun, Yuan; Xie, Qing-Ge

doi:10.1016/j.vetimm.2007.08.010

Cited by 45 publications

(19 citation statements)

References 21 publications

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“…The value of ER retention has been previously demonstrated where a ER retention signal increased human anti-HIV 2G12 levels in N. benthamiana plants 28 . Higher expression of ER-retained proteins has also been demonstrated for a structural poly-protein, P1–2A, as well as for a 3C protease from FMDV serotype O when stably expressed in foliar tomato extract 29 . In contrast, when a signal peptide such as the CTB signal peptide is absent, expression of the viral protein is not detectable possibly due to degradation within the cytoplasm during, or immediately after, synthesis 30 .…”

Section: Selecting the Cellular Compartment For Recombinant Productionmentioning

confidence: 84%

Proteolysis of recombinant proteins in bioengineered plant cells

et al. 2013

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Plants are increasingly used as alternative expression hosts for the production of recombinant proteins offering many advantages including higher biomass and the ability to perform post-translational modifications on complex proteins. Key challenges for optimized accumulation of recombinant proteins in a plant system still remain, including endogenous plant proteolytic activity, which may severely compromise recombinant protein stability. Several strategies have recently been applied to improve protein stability by limiting protease action such as recombinant protein production in various sub-cellular compartments or application of protease inhibitors to limit protease action. A short update on the current strategies applied is provided here, with particular focus on sub-cellular sites previously selected for recombinant protein production and the co-expression of protease inhibitors to limit protease activity.

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Section: Selecting the Cellular Compartment For Recombinant Productionmentioning

confidence: 84%

Proteolysis of recombinant proteins in bioengineered plant cells

et al. 2013

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“…The transgenic tomato plants were Sharma et al (2008b) also used to express the structural polyprotein P1-2A and protease 3C from FMDV. Guinea pigs immunized intramuscularly with foliar extracts from P1-2A3C-transgenic tomato plants were found to develop a virus-specific antibody response against FMDV (Pan et al 2008). A single-chain variable antibody fragment (scFv) recognizing FMDV coat protein VP1 was expressed in transgenic tobacco plants.…”

Section: Viral Vaccinementioning

confidence: 99%

Recent advances and safety issues of transgenic plant-derived vaccines

Guan

Guo

Huo

et al. 2013

Appl Microbiol Biotechnol

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Transgenic plant-derived vaccines comprise a new type of bioreactor that combines plant genetic engineering technology with an organism's immunological response. This combination can be considered as a bioreactor that is produced by introducing foreign genes into plants that elicit special immunogenicity when introduced into animals or human beings. In comparison with traditional vaccines, plant vaccines have some significant advantages, such as low cost, greater safety, and greater effectiveness. In a number of recent studies, antigen-specific proteins have been successfully expressed in various plant tissues and have even been tested in animals and human beings. Therefore, edible vaccines of transgenic plants have a bright future. This review begins with a discussion of the immune mechanism and expression systems for transgenic plant vaccines. Then, current advances in different transgenic plant vaccines will be analyzed, including vaccines against pathogenic viruses, bacteria, and eukaryotic parasites. In view of the low expression levels for antigens in plants, high-level expression strategies of foreign protein in transgenic plants are recommended. Finally, the existing safety problems in transgenic plant vaccines were put forward will be discussed along with a number of appropriate solutions that will hopefully lead to future clinical application of edible plant vaccines.

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“…The 3C protease is one of many non-structural proteins synthesised in the infected cell but expression of P1-2A and 3C in the absence of any other FMDV encoded protein in recombinant systems is sufficient to afford authentic precursor cleavage (Lewis et al, 1991; Roosien et al, 1990). Accordingly there have been a number of reports of the assembly of recombinant FMDV empty capsids following the use of expression systems such as vaccinia virus (Abrams et al, 1995), adenovirus (Mason et al, 2003), E. coli (Cao et al, 2010; Lewis et al, 1991), transgenic plants (Pan et al, 2008) and baculovirus (Li et al, 2008; Oem et al, 2007; Roosien et al, 1990). In some cases, sufficient empty capsid material has been prepared to immunise cattle and protection against homologous challenge was demonstrated (Li et al, 2008, 2011) but in the main the configuration of the P1and 3C coding sequences used to achieve empty capsid expression and the efficiency of capsid assembly has been highly variable, particularly in insect cells.…”

Section: Introductionmentioning

confidence: 99%

Efficient production of foot-and-mouth disease virus empty capsids in insect cells following down regulation of 3C protease activity

Porta

Loureiro

et al. 2013

Journal of Virological Methods

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Highlights► Efficient expression of FMDV empty capsids in insect cells after moderation of 3C protease action. ► Expression cassette productive in multiple insect cell lines. ► Empty capsids visualised by transmission electron microscopy. ► Empty capsids react with wide range of positive sera as well as authentic virus. ► Efficient empty capsid synthesis may allow development as a vaccine.

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Foliar extracts from transgenic tomato plants expressing the structural polyprotein, P1-2A, and protease, 3C, from foot-and-mouth disease virus elicit a protective response in guinea pigs

Cited by 45 publications

References 21 publications

Proteolysis of recombinant proteins in bioengineered plant cells

Proteolysis of recombinant proteins in bioengineered plant cells

Recent advances and safety issues of transgenic plant-derived vaccines

Efficient production of foot-and-mouth disease virus empty capsids in insect cells following down regulation of 3C protease activity

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