ReviewApplied microbiology and biotechnology2021
Engineering of the unfolded protein response pathway in Pichia pastoris: enhancing production of secreted recombinant proteins.
Review in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled it.
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Who cites it
56 citing papers in PubMed, 1 synthesis or guideline pooled it.
- A Systematic Review of the Potential of Pichia pastoris (Komagataella phaffii) as an Alternative Host for Biologics Production.Molecular biotechnology · 2024Pooled it
- Constructing an efficient synthesis pathway in peroxisomes to boostSynthetic and systems biotechnology · 2026Article
- Metabolic engineering ofApplied and environmental microbiology · 2026Review
- Development and optimization of a glycerol-based fed-batch strategy for the production of peroxidases with Komagataella phaffii under the PMicrobial cell factories · 2026Article
- Improvement of cannabichromenic acid synthase activity and construction of recombinant yeast strain.Archives of microbiology · 2026Article
- Engineering sweetness: zeocin-based strain screening to identify high-titerFood science and biotechnology · 2026Article
- Pichia Toolkit: Use of the combinatorial library screening system for expression of a marine laccase.Folia microbiologica · 2026Article
- Characterizing the role of an endogenous serine protease KpSub2 in recombinant collagen degradation in Komagataella phaffii.Bioresources and bioprocessing · 2026Article
- EstablishingBiodesign research · 2026Article
- Systematic perturbation of cultures of K. phaffii by carbon co-feeding show gene signatures associated with production of recombinant proteins.Microbial cell factories · 2026Article
- Efficient Expression of Lactone Hydrolase Cr2zen for Scalable Zearalenone Degradation inToxins · 2025Article
- High-level expression of zearalenone lactonohydrolase ZenG in Pichia pastoris via combinatorial strategy.Archives of microbiology · 2025Article
- Potential of a constitutive-UPR and histone deacetylase A-deficientApplied and environmental microbiology · 2025Article
- Article
- Recombinant DNA the Bio-Revolution, Between Promise, Hurdles, and Achievements.International journal of molecular sciences · 2025Article
- The MFα signal sequence in yeast-based protein secretion: challenges and innovations'.Applied microbiology and biotechnology · 2025Review
- Structural Homology Fails to Predict Secretion Efficiency inInternational journal of molecular sciences · 2025Article
- Production and application of peptidyl-lys metalloendopeptidase: advances, challenges, and future perspectives.Applied microbiology and biotechnology · 2025Review
- Expression and characterization of cold-adapted xylanase Xyl-L in Pichia pastoris for xylooligosaccharide (XOS) preparation.Microbial cell factories · 2025Article
- Effect of Fold-Promoting Mutation and Signal Peptide Screening on Recombinant Glucan 1,4-Alpha-maltohydrolase Secretion in Pichia pastoris.Applied biochemistry and biotechnology · 2025Article
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5 authors.
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Abstract
Folding and processing of proteins in the endoplasmic reticulum (ER) are major impediments in the production and secretion of proteins from Pichia pastoris (Komagataella sp.). Overexpression of recombinant genes can overwhelm the innate secretory machinery of the P. pastoris cell, and incorrectly folded proteins may accumulate inside the ER. To restore proper protein folding, the cell naturally triggers an unfolded protein response (UPR) pathway, which upregulates the expression of genes coding for chaperones and other folding-assisting proteins (e.g., Kar2p, Pdi1, Ero1p) via the transcription activator Hac1p. Unfolded/misfolded proteins that cannot be repaired are degraded via the ER-associated degradation (ERAD) pathway, which decreases productivity. Co-expression of selected UPR genes, along with the recombinant gene of interest, is a common approach to enhance the production of properly folded, secreted proteins. Such an approach, however, is not always successful and sometimes, protein productivity decreases because of an unbalanced UPR. This review summarizes successful chaperone co-expression strategies in P. pastoris that are specifically related to overproduction of foreign proteins and the UPR. In addition, it illustrates possible negative effects on the cell's physiology and productivity resulting from genetic engineering of the UPR pathway. We have focused on Pichia's potential for commercial production of valuable proteins and we aim to optimize molecular designs so that production strains can be tailored to suit a specific heterologous product. KEY POINTS: • Chaperones co-expressed with recombinant genes affect productivity in P. pastoris. • Enhanced UPR may impair strain physiology and promote protein degradation. • Gene copy number of the target gene and the chaperone determine the secretion rate.
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