ArticleMicrobial cell factories2018
An improved secretion signal enhances the secretion of model proteins from Pichia pastoris.
Article in Microbial cell factories, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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63 citing papers in PubMed, 152 citations in OpenAlex.
- Yarrowia lipolytica and Komagataella phaffii (Pichia pastoris) as Hosts for Heterologous Expression of Lipases.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Systematic optimization ofEngineering microbiology · 2026Review
- Heterologous expression of hagfish thread proteins EsTKα and EsTKγ inSynthetic and systems biotechnology · 2026Article
- Enhanced biosynthesis of full-length triple-helical human type III collagen in engineered Komagataella phaffii.Applied microbiology and biotechnology · 2026Article
- Advances in Key Genetic Elements and Strategies for High-Yield Heterologous Protein Expression inJournal of fungi (Basel, Switzerland) · 2026Review
- Recombinant Expression of Chitinase CtChi70 in Komagataella phaffii for Sustainable N, N'-Diacetyl-Chitobiose Production From Shrimp Shells.Biotechnology journal · 2026Article
- Enhanced secretion of an Agrocybe aegerita peroxygenase variant in K. phaffii using the native signal peptide.AMB Express · 2026Article
- Effect of Different Signal Peptides on the Expression of Glucoamylase fromJournal of fungi (Basel, Switzerland) · 2026Article
- A chimeric rather than native secretion signal elicits stress-related transcriptional adaption during 75k γ-secalin production inFEMS microbes · 2026Article
- High-level expression of zearalenone lactonohydrolase ZenG in Pichia pastoris via combinatorial strategy.Archives of microbiology · 2025Article
- PIONEER: A Periplasmic Display Platform for Synthetic Biology-Based Screening of Genetically Encoded Protein Regulators.bioRxiv : the preprint server for biology · 2025Article
- Lipid bilayer thinning near a ubiquitin ligase selects ER membrane proteins for degradation.bioRxiv : the preprint server for biology · 2025Article
- Recent advances in microbial fermentation for the production of leghemoglobin.World journal of microbiology & biotechnology · 2025Review
- Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii.Applied microbiology and biotechnology · 2025Article
- Oral Immunization with Yeast-Surface Display of SARS-CoV-2 Antigens inInfectious disease reports · 2025Article
- Higher induction temperatures and the native secretion signal peptide promote rye prolamin 75k γ-secalin production in Komagataella phaffii.Microbial cell factories · 2025Article
- The MFα signal sequence in yeast-based protein secretion: challenges and innovations'.Applied microbiology and biotechnology · 2025Review
- High-efficiency patatin expression strategies inSynthetic and systems biotechnology · 2025Article
- Impact of Oxygen Availability on the Organelle-Specific Redox Potentials and Stress in Recombinant Protein Producing Komagataella phaffii.Microbial biotechnology · 2025Article
- Adaptation of Aglycosylated Monoclonal Antibodies for Improved Production in Komagataella phaffii.Biotechnology and bioengineering · 2025Article
3 more citing papers are in PubMed but not listed here.
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5 authors at 2 institutions in 3 countries.
Funding
Abstract
backgroundProteins can be secreted from a host organism with the aid of N-terminal secretion signals. The budding yeast Pichia pastoris (Komagataella sp.) is widely employed to secrete proteins of academic and industrial interest. For this yeast, the most commonly used secretion signal is the N-terminal portion of pre-pro-α-factor from Saccharomyces cerevisiae. However, this secretion signal promotes posttranslational translocation into the endoplasmic reticulum (ER), so proteins that can fold in the cytosol may be inefficiently translocated and thus poorly secreted. In addition, if a protein self-associates, the α-factor pro region can potentially cause aggregation, thereby hampering export from the ER. This study addresses both limitations of the pre-pro-α-factor secretion signal.
resultsWe engineered a hybrid secretion signal consisting of the S. cerevisiae Ost1 signal sequence, which promotes cotranslational translocation into the ER, followed by the α-factor pro region. Secretion and intracellular localization were assessed using as a model protein the tetrameric red fluorescent protein E2-Crimson. When paired with the α-factor pro region, the Ost1 signal sequence yielded much more efficient secretion than the α-factor signal sequence. Moreover, an allelic variant of the α-factor pro region reduced aggregation of the E2-Crimson construct in the ER. The resulting improved secretion signal enhanced secretion of E2-Crimson up to 20-fold compared to the levels obtained with the original α-factor secretion signal. Similar findings were obtained with the lipase BTL2, which exhibited 10-fold enhanced secretion with the improved secretion signal.
conclusionsThe improved secretion signal confers dramatic benefits for the secretion of certain proteins from P. pastoris. These benefits are likely to be most evident for proteins that can fold in the cytosol and for oligomeric proteins.
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