ArticlePloS one2013
Enhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1' site.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 76 citations in OpenAlex.
- Systematic optimization ofEngineering microbiology · 2026Review
- A New Strategy of Alternating Current Magnetic Field-Assisted Three-Phase Partitioning (ACMF-TPP) for the Concentration and Partial Purification of Recombinant Prepromelittin Produced by Komagataella phaffii.Biotechnology and applied biochemistry · 2026Article
- The MFα signal sequence in yeast-based protein secretion: challenges and innovations'.Applied microbiology and biotechnology · 2025Review
- Review
- Molecular Modification of Kex2 P1' Site Enhances Expression and Druggability of Fungal Defensin.Antibiotics (Basel, Switzerland) · 2023Article
- Structural and Functional Analysis of Peptides Derived from KEX2-Processed Repeat Proteins in Agaricomycetes Using Reverse Genetics and Peptidomics.Microbiology spectrum · 2022Article
- Production of autolysis-proof Kex2 protease from Candida albicans in Saccharomyces cerevisiae for in vitro processing of fusion proteins.Applied microbiology and biotechnology · 2022Article
- Molecular advances in microbial α-galactosidases: challenges and prospects.World journal of microbiology & biotechnology · 2022Review
- Modifications in the Kex2 P1' cleavage site in the α-MAT secretion signal lead to higher production of human granulocyte colony-stimulating factor in Pichia pastoris.World journal of microbiology & biotechnology · 2021Article
- Buried Kex2 Sites in Glargine Precursor Aggregates Prevent Its Intracellular Processing in Pichia pastoris MutApplied biochemistry and biotechnology · 2021Article
- Review
- Platforms for Production of Protein-Based Vaccines: From Classical to Next-Generation Strategies.Biomolecules · 2021Review
- Production of Industrial Enzymes via Pichia pastoris as a Cell Factory in Bioreactor: Current Status and Future Aspects.The protein journal · 2021Review
- Design of an improved universal signal peptide based on the α-factor mating secretion signal for enzyme production in yeast.Cellular and molecular life sciences : CMLS · 2021Article
- Comparison of the secretory murine DNase1 family members expressed in Pichia pastoris.PloS one · 2021Article
- Artificial Transcription Factors for Tuneable Gene Expression inFrontiers in bioengineering and biotechnology · 2021Article
- Differential role of segments of α-mating factor secretion signal in Pichia pastoris towards granulocyte colony-stimulating factor emerging from a wild type or codon optimized copy of the gene.Microbial cell factories · 2020Article
- Pichia pastoris: A highly successful expression system for optimal synthesis of heterologous proteins.Journal of cellular physiology · 2020Review
- Review
- Enzymatic activity of a recombinant β-1,4-endoglucanase from the Cotton Boll Weevil (Anthonomus grandis) aiming second generation ethanol production.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
13 authors at 7 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pichiapastoris is one of the most widely used expression systems for the production of recombinant secretory proteins. Its universal application is, however, somewhat hampered by its unpredictable yields for different heterologous proteins, which is now believed to be caused in part by their varied efficiencies to traffic through the host secretion machinery. The yeast endoprotease Kex2 removes the signal peptides from pre-proteins and releases the mature form of secreted proteins, thus, plays a pivotal role in the yeast secretory pathways. In this study, we found that the yields of many recombinant proteins were greatly influenced by Kex2 P1' site residues and the optimized P1's amino acid residue could largely determine the final amount of secretory proteins synthesized and secreted. A further improvement of secretory yield was achieved by genomic integration of additional Kex2 copies, which again highlighted the importance of Kex2 cleavage to the production of recombinant secretory proteins in Pichia yeast.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.