ArticlePlant physiology2010
Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana.
Article in Plant physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 193 citations in OpenAlex.
- Design and Immunogenicity of a Nanoparticle Combination Vaccine for Salmonella in Poultry.Plant biotechnology journal · 2026Article
- A synthetic expression system for orthogonal gene expression in Nicotiana benthamiana.Plant molecular biology · 2026Article
- Advancing the frontier of plant-based therapeutics: critical innovations in molecular farming and bioprocess Integration.Biotechnology letters · 2026Review
- Protein engineering strategies to optimise recombinant product synthesis and accumulation in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Hydrophobin-Fused SARS-CoV-2 RBD production inFuture science OA · 2025Article
- Article
- A conserved lysine/arginine-rich motif is essential for the autophagic degradation of potyviral 6K1 protein and virus infection.Journal of virology · 2025Article
- Transient Expression of Zika NS2B Protein Antigen inACS omega · 2025Article
- Expression and Characterization of Alkaline Phosphatase fromPlants (Basel, Switzerland) · 2024Article
- Improving glucose oxidase catalysis in Aspergillus niger via Vitreoscilla hemoglobin fusion protein.Applied microbiology and biotechnology · 2024Article
- Rubisco small subunit (RbCS) is co-opted by potyvirids as the scaffold protein in assembling a complex for viral intercellular movement.PLoS pathogens · 2024Article
- Review
- A Zinc Finger Motif in the P1 N Terminus, Highly Conserved in a Subset of Potyviruses, Is Associated with the Host Range and Fitness of Telosma Mosaic Virus.Journal of virology · 2023Article
- Development of a tag-free plant-made interferon gamma production system with improved therapeutic efficacy against viruses.Frontiers in bioengineering and biotechnology · 2023Article
- Performance of plant-produced RBDs as SARS-CoV-2 diagnostic reagents: a tale of two plant platforms.Frontiers in plant science · 2023Article
- Recent advances in expression and purification strategies for plant made vaccines.Frontiers in plant science · 2023Review
- Increasing the Efficiency of the Accumulation of Recombinant Proteins in Plant Cells: The Role of Transport Signal Peptides.Plants (Basel, Switzerland) · 2022Review
- Insights into the trihelix transcription factor responses to salt and other stresses in Osmanthus fragrans.BMC genomics · 2022Article
- Specialized endoplasmic reticulum-derived vesicles in plants: Functional diversity, evolution, and biotechnological exploitation.Journal of integrative plant biology · 2022Review
- Improving Protein Quantity and Quality-The Next Level of Plant Molecular Farming.International journal of molecular sciences · 2022Review
13 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insufficient accumulation levels of recombinant proteins in plants and the lack of efficient purification methods for recovering these valuable proteins have hindered the development of plant biotechnology applications. Hydrophobins are small and surface-active proteins derived from filamentous fungi that can be easily purified by a surfactant-based aqueous two-phase system. In this study, the hydrophobin HFBI sequence from Trichoderma reesei was fused to green fluorescent protein (GFP) and transiently expressed in Nicotiana benthamiana plants by Agrobacterium tumefaciens infiltration. The HFBI fusion significantly enhanced the accumulation of GFP, with the concentration of the fusion protein reaching 51% of total soluble protein, while also delaying necrosis of the infiltrated leaves. Furthermore, the endoplasmic reticulum-targeted GFP-HFBI fusion induced the formation of large novel protein bodies. A simple and scalable surfactant-based aqueous two-phase system was optimized to recover the HFBI fusion proteins from leaf extracts. The single-step phase separation was able to selectively recover up to 91% of the GFP-HFBI up to concentrations of 10 mg mL(-1). HFBI fusions increased the expression levels of plant-made recombinant proteins while also providing a simple means for their subsequent purification. This hydrophobin fusion technology, when combined with the speed and posttranslational modification capabilities of plants, enhances the value of transient plant-based expression systems.
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