ArticlePLoS biology2022
Identification of genetic variants of the industrial yeast Komagataella phaffii (Pichia pastoris) that contribute to increased yields of secreted heterologous proteins.
Article in PLoS biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 26 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
- Pichia pastoris Genomic Resources: Accessibility, Recommendations, and Pitfalls.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Decoding the Genome of the Komagataella phaffii Type Strain CBS 2612.Yeast (Chichester, England) · 2025Article
- Development of a Komagataella phaffii cell factory for sustainable production of ( +)-valencene.Microbial cell factories · 2025Article
- Hansenula polymorpha methanol metabolism genes enhance recombinant protein production in Komagataella phaffi.AMB Express · 2024Article
- Understanding exopolysaccharide byproduct formation in Komagataella phaffii fermentation processes for recombinant protein production.Microbial cell factories · 2024Article
- OPENPichia: licence-free Komagataella phaffii chassis strains and toolkit for protein expression.Nature microbiology · 2024Article
- Review
- Characterization of the exopolysaccharides produced by the industrial yeast Komagataella phaffii.Journal of industrial microbiology & biotechnology · 2024Article
- Characterising the metabolic rewiring of extremely slow growing Komagataella phaffii.Microbial biotechnology · 2024Article
- Exploring the genetic architecture of protein secretion in Komagataella phaffii (Pichia pastoris) for biotechnology applications.PLoS biology · 2022Article
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7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast Komagataella phaffii (formerly called Pichia pastoris) is used widely as a host for secretion of heterologous proteins, but only a few isolates of this species exist and all the commonly used expression systems are derived from a single genetic background, CBS7435 (NRRL Y-11430). We hypothesized that other genetic backgrounds could harbor variants that affect yields of secreted proteins. We crossed CBS7435 with 2 other K. phaffii isolates and mapped quantitative trait loci (QTLs) for secretion of a heterologous protein, β-glucosidase, by sequencing individual segregant genomes. A major QTL mapped to a frameshift mutation in the mannosyltransferase gene HOC1, which gives CBS7435 a weaker cell wall and higher protein secretion than the other isolates. Inactivation of HOC1 in the other isolates doubled β-glucosidase secretion. A second QTL mapped to an amino acid substitution in IRA1 that tripled β-glucosidase secretion in 1-week batch cultures but reduced cell viability, and its effects are specific to this heterologous protein. Our results demonstrate that QTL analysis is a powerful method for dissecting the basis of biotechnological traits in nonconventional yeasts, and a route to improving their industrial performance.
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