ArticleMicrobial cell factories2023
Improving expression and assembly of difficult-to-express heterologous proteins in Saccharomyces cerevisiae by culturing at a sub-physiological temperature.
Article in Microbial cell factories, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Integrated Fermentation Engineering Enables High-Level Leghemoglobin Production in Kluyveromyces marxianus via Metabolic Rewiring of Central Carbon Metabolism and Amino Acid Utilization.Biotechnology journal · 2026Article
- Metabolic Engineering ofJournal of fungi (Basel, Switzerland) · 2026Article
- Alleviation of ER stress via targeted genetic engineering enhances recombinant ovalbumin secretion inFood science and biotechnology · 2026Article
- Cell surface display of VP1 of foot-and-mouth disease virus on Saccharomyces cerevisiae.Microbial cell factories · 2025Article
- Expression of Recombinant Hirudin in Bacteria and Yeast: A Comparative Approach.Methods and protocols · 2025Article
- Article
- Recent perspectives on biotechnological production, modulation and applications of glycerophosphoryl diester phosphodiesterases.Biodegradation · 2025Review
- Metabolic engineering of Saccharomyces cerevisiae for the biosynthesis of a fungal pigment from the phytopathogenic fungus Cladosporium phlei.Journal of biological engineering · 2024Article
- Combinatorial optimization of pathway, process and media for the production of p-coumaric acid by Saccharomyces cerevisiae.Microbial biotechnology · 2024Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundEscherichia coli heat labile toxin B subunit (LTB) is one of the most popular oral vaccine adjuvants and intestine adsorption enhancers. It is often expressed as a fusion partner with target antigens to enhance their immunogenicity as well as gut absorbability. However, high expression levels of a fusion protein are critical to the outcome of immunization experiments and the success of subsequent vaccine development efforts. In order to improve the expression and functional assembly of LTB-fusion proteins using Saccharomyces cerevisiae, we compared their expression under culture conditions at a sub-physiological temperature 20 °C with their expression under a standard 30 °C.
resultsThe assembled expression of LTB-EDIII
conclusionsThe effects of lowering the expression temperature from 30 °C to 20 °C on protein expression and folding levels in S. cerevisiae, using several proteins as models, are reported. When heterologous proteins are expressed at 20 °C, a greater amount of (specially, more assembled) functional proteins accumulated than at 30 °C. Although further studies are required to understand the molecular mechanisms, our results suggest that lowering the expression temperature is a convenient strategy for improving the expression of relatively complexly structured and difficult-to-express proteins in S. cerevisiae.
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