ArticlePloS one2016
Novel Hydrophobin Fusion Tags for Plant-Produced Fusion Proteins.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- A synthetic expression system for orthogonal gene expression in Nicotiana benthamiana.Plant molecular biology · 2026Article
- 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
- Transient Expression of Zika NS2B Protein Antigen inACS omega · 2025Article
- Plant Expression of Hydrophobin Fused K39 Antigen for Visceral Leishmaniasis Immunodiagnosis.Frontiers in plant science · 2021Article
- Advances in Plant-Derived Scaffold Proteins.Frontiers in plant science · 2020Review
- Hydrophobins: multifunctional biosurfactants for interface engineering.Journal of biological engineering · 2019Review
- What We Do Not Know about Fungal Cell Adhesion Molecules.Journal of fungi (Basel, Switzerland) · 2018Review
- Cytosolic and Nuclear Co-localization of Betalain Biosynthetic Enzymes in Tobacco Suggests that Betalains Are Synthesized in the Cytoplasm and/or Nucleus of Betalainic Plant Cells.Frontiers in plant science · 2017Article
- Subcellular Localization of a Plant Catalase-Phenol Oxidase, AcCATPO, fromFrontiers in plant science · 2017Article
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4 authors.
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Abstract
Hydrophobin fusion technology has been applied in the expression of several recombinant proteins in plants. Until now, the technology has relied exclusively on the Trichoderma reesei hydrophobin HFBI. We screened eight novel hydrophobin tags, T. reesei HFBII, HFBIII, HFBIV, HFBV, HFBVI and Fusarium verticillioides derived HYD3, HYD4 and HYD5, for production of fusion proteins in plants and purification by two-phase separation. To study the properties of the hydrophobins, we used N-terminal and C-terminal GFP as a fusion partner. Transient expression of the hydrophobin fusions in Nicotiana benthamiana revealed large variability in accumulation levels, which was also reflected in formation of protein bodies. In two-phase separations, only HFBII and HFBIV were able to concentrate GFP into the surfactant phase from a plant extract. The separation efficiency of both tags was comparable to HFBI. When the accumulation was tested side by side, HFBII-GFP gave a better yield than HFBI-GFP, while the yield of HFBIV-GFP remained lower. Thus we present here two alternatives for HFBI as functional fusion tags for plant-based protein production and first step purification.
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