ArticleJournal of experimental botany2009
A bacterial signal peptide is functional in plants and directs proteins to the secretory pathway.
Article in Journal of experimental botany, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- An Interplay between Mitochondrial and ER Targeting of a Bacterial Signal Peptide in Plants.Plants (Basel, Switzerland) · 2023Article
- HrpE, the major component of the Xanthomonas type three protein secretion pilus, elicits plant immunity responses.Scientific reports · 2018Article
- The lysin motif-containing proteins, Lyp1, Lyk7 and LysMe3, play important roles in chitin perception and defense against Verticillium dahliae in cotton.BMC plant biology · 2017Article
- Expression of Foreign Genes Demonstrates the Effectiveness of Pollen-Mediated Transformation inFrontiers in plant science · 2017Article
- Oral immunisation of mice with transgenic rice calli expressing cholera toxin B subunit fused to consensus dengue cEDIII antigen induces antibodies to all four dengue serotypes.Plant molecular biology · 2016Article
- Expression of H3N2 nucleoprotein in maize seeds and immunogenicity in mice.Plant cell reports · 2015Article
- Recent advances on host plants and expression cassettes' structure and function in plant molecular pharming.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2014Review
- Ectopic expression of bacterial amylopullulanase enhances bioethanol production from maize grain.Plant cell reports · 2013Article
- Expression of the cholera toxin B subunit (CT-B) in maize seeds and a combined mucosal treatment against cholera and traveler's diarrhea.Plant cell reports · 2012Article
- A plant secretory signal peptide targets plastome-encoded recombinant proteins to the thylakoid membrane.Plant molecular biology · 2011Article
- Article
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3 authors.
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Abstract
The Escherichia coli heat-labile enterotoxin B subunit (LT-B) has been used as a model antigen for the production of plant-derived high-valued proteins in maize. LT-B with its native signal peptide (BSP) has been shown to accumulate in starch granules of transgenic maize kernels. To elucidate the targeting properties of the bacterial LT-B protein and BSP in plant systems, the subcellular localization of visual marker green fluorescent protein (GFP) fused to LT-B and various combinations of signal peptides was examined in Arabidopsis protoplasts and transgenic maize. Biochemical analysis indicates that the LT-B::GFP fusion proteins can assemble and fold properly retaining both the antigenicity of LT-B and the fluorescing properties of GFP. Maize kernel fractionation revealed that transgenic lines carrying BSP result in recombinant protein association with fibre and starch fractions. Confocal microscopy analysis indicates that the fusion proteins accumulate in the endomembrane system of plant cells in a signal peptide-dependent fashion. This is the first report providing evidence of the ability of a bacterial signal peptide to target proteins to the plant secretory pathway. The results provide important insights for further understanding the heterologous protein trafficking mechanisms and for developing effective strategies in molecular farming.
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