ArticleInternational archives of allergy and immunology2017
Expression and Characterization of Functional Recombinant Bet v 1.0101 in the Chloroplast of Chlamydomonas reinhardtii.
Article in International archives of allergy and immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 43 citations in OpenAlex.
- Process intensification for the protein production from microalgae: a comprehensive review.Bioresources and bioprocessing · 2026Review
- Harnessing the potential of microalgae for the production of monoclonal antibodies and other recombinant proteins.Protoplasma · 2024Review
- The red algaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Current Status and Perspective on the Use of Viral-Based Vectors in Eukaryotic Microalgae.Marine drugs · 2022Review
- Emerging Trends in Genetic Engineering of Microalgae for Commercial Applications.Marine drugs · 2022Review
- Harnessing the Algal Chloroplast for Heterologous Protein Production.Microorganisms · 2022Review
- High-Yield Production of the Major Birch Pollen Allergen Bet v 1 With Allergen Immunogenicity inFrontiers in plant science · 2020Article
- Review
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundAllergen immunotherapy (AIT) still plays a minor role in the treatment of allergic diseases. To improve the acceptance of AIT by allergic patients, the treatment has to become more convenient and efficacious. One possibility is the oral application of allergens or derivatives thereof. Therefore, we sought to produce a recombinant allergen in the green alga Chlamydomonas reinhardtii as a novel production platform.
methodsThe major birch pollen allergen Bet v 1 was selected as candidate molecule, and a codon-optimized gene was synthesized and stably integrated into the microalga C. reinhardtii FUD50. Positive transformants were identified by PCR, cultured, and thereafter cells were disrupted by sonication. Bet v 1 was purified from algal total soluble protein (TSP) by affinity chromatography and characterized physicochemically as well as immunologically.
resultsAll transformants showed expression of the allergen with yields between 0.01 and 0.04% of TSP. Algal-derived Bet v 1 displayed similar secondary structure elements as the Escherichia coli-produced reference allergen. Moreover, Bet v 1 produced in C. reinhardtii showed binding comparable to human IgE as well as murine Bet v 1-specific IgG.
conclusionWe could successfully produce recombinant Bet v 1 in C. reinhardtii. As microalgae are classified as GRAS (generally recognized as safe), the pilot study supports the development of novel allergy treatment concepts such as the oral administration of allergen-containing algal extracts for therapy.
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