Immunogenicity and contraceptive efficacy of plant-produced putative mouse-specific contraceptive peptides.

Rodent population control through contraception requires species-specific oral contraceptive vaccines. Therefore, in this study, we produced putative mouse-specific contraceptive peptides, mZP2 (from oocyte) and mIzumo1 (from sperm), in plants using -mediated transient expression. Peptides were produced separately in using constructs encoding antigens containing three copies of each peptide.

Oral and Subcutaneous Immunization with a Plant-Produced Mouse-Specific Zona Pellucida 3 Peptide Presented on Hepatitis B Core Antigen Virus-like Particles.

A short mouse-specific peptide from zona pellucida 3 (mZP3, amino acids 328-342) has been shown to be associated with antibody-mediated contraception. In this study, we investigated the production of mZP3 in the plant, as an orally applicable host, and examined the immunogenicity of this small peptide in the BALB/c mouse model. The mZP3 peptide was inserted into the major immunodominant region of the hepatitis B core antigen and was produced in plants via -mediated transient expression.

Plant-Produced Mouse-Specific Zona Pellucida 3 Peptide Induces Immune Responses in Mice.

Contraceptive vaccines are designed to stimulate autoimmune responses to molecules involved in the reproductive process. A mouse-specific peptide from zona pellucida 3 (mZP3) has been proposed as a target epitope. Here, we employed a plant expression system for the production of glycosylated mZP3 and evaluated the immunogenicity of plant-produced mZP3-based antigens in a female BALB/c mouse model.

Seed- and leaf-based expression of FGF21-transferrin fusion proteins for oral delivery and treatment of non-alcoholic steatohepatitis.

Non-alcoholic steatohepatitis (NASH) is a global disease with no effective medication. The fibroblast growth factor 21 (FGF21) can reverse this liver dysfunction, but requires targeted delivery to the liver, which can be achieved oral administration. Therefore, we fused FGF21 to transferrin (Tf) a furin cleavage site (F), to promote uptake from the intestine into the portal vein, yielding FGF21-F-Tf, and established its production in both seeds and leaves of commercial cultivars, compared their expression profile and tested the bioavailability and bioactivity in feeding studies.

Corrigendum: Sustainable production of the cyanophycin biopolymer in tobacco in the greenhouse and field.

[This corrects the article DOI: 10.3389/fbioe.2022.

Sustainable Production of the Cyanophycin Biopolymer in Tobacco in the Greenhouse and Field.

The production of biodegradable polymers as coproducts of other commercially relevant plant components can be a sustainable strategy to decrease the carbon footprint and increase the commercial value of a plant. The biodegradable polymer cyanophycin granular polypeptide (CGP) was expressed in the leaves of a commercial tobacco variety, whose seeds can serve as a source for biofuel and feed. In T0 generation in the greenhouse, up to 11% of the leaf dry weight corresponded to the CGP.

KP4 to control in wheat: Enhanced greenhouse resistance to loose smut and changes in transcript abundance of pathogen related genes in infected KP4 plants.

causes loose smut, which is a seed-borne fungal disease of wheat, and responsible for yield losses up to 40%. Loose smut is a threat to seed production in developing countries where small scale farmers use their own harvest as seed material. The killer protein 4 (KP4) is a virally encoded toxin from and inhibits growth of susceptible races of fungi from the Ustilaginales.

Peculiarities and impacts of expression of bacterial cyanophycin synthetases in plants.

Cyanophycin (CP) can be successfully produced in plants by the ectopic expression of the CphA synthetase from Thermosynechococcus elongatus BP-1 (Berg et al. 2000), yielding up to 6.8 % of dry weight (DW) in tobacco leaf tissue and 7.

Recombinant production of human interleukin 6 in Escherichia coli.

In this study, we compared basic expression approaches for the efficient expression of bioactive recombinant human interleukin-6 (IL6), as an example for a difficult-to-express protein. We tested these approaches in a laboratory scale in order to pioneer the commercial production of this protein in Escherichia coli (E. coli).

Expression and subcellular targeting of human complement factor C5a in Nicotiana species.

We evaluated transgenic tobacco plants as an alternative to Escherichia coli for the production of recombinant human complement factor 5a (C5a). C5a has not been expressed in plants before and is highly unstable in vivo in its native form, so it was necessary to establish the most suitable subcellular targeting strategy. We used the strong and constitutive CaMV 35S promoter to drive transgene expression and compared three different subcellular compartments.

High-level transient expression of ER-targeted human interleukin 6 in Nicotiana benthamiana.

Tobacco plants can be used to express recombinant proteins that cannot be produced in a soluble and active form using traditional platforms such as Escherichia coli. We therefore expressed the human glycoprotein interleukin 6 (IL6) in two commercial tobacco cultivars (Nicotiana tabacum cv. Virginia and cv.

A membrane-bound FtsH protease is involved in osmoregulation in Synechocystis sp. PCC 6803: the compatible solute synthesizing enzyme GgpS is one of the targets for proteolysis.

Protein quality control and proteolysis are involved in cell maintenance and environmental acclimatization in bacteria and eukaryotes. The AAA protease FtsH2 of the cyanobacterium Synechocystis sp. PCC 6803 was identified during a screening for mutants impaired in osmoregulation.

Proteome analysis of salt stress response in the cyanobacterium Synechocystis sp. strain PCC 6803.

In the present study, changes in protein synthesis patterns after salt shock visualized by 35S-methionine labeling and the changed protein composition in salt-acclimated cells of the cyanobacterium Synechocystis sp. strain PCC 6803 were analyzed by a combination of 2-DE for protein separation and PMF for protein identification. As a basis for the differential analysis, a proteome map with 500 identified protein spots comprising 337 different protein species was established.

Salt-dependent expression of glucosylglycerol-phosphate synthase, involved in osmolyte synthesis in the cyanobacterium Synechocystis sp. strain PCC 6803.

The cyanobacterium Synechocystis sp. strain PCC 6803 is able to acclimate to levels of salinity ranging from freshwater to twice the seawater concentrations of salt by accumulating the compatible solute glucosylglycerol (GG). Expression of the ggpS gene coding for the key enzyme (glucosylglycerol-phosphate synthase) in GG synthesis was examined in detail.

Stress responses of Synechocystis sp. strain PCC 6803 mutants impaired in genes encoding putative alternative sigma factors.

In the complete genome sequence of the cyanobacterium SYNECHOCYSTIS: sp. strain PCC 6803 [Kaneko et al. (1996 ).