ArticleMicrobial cell factories2023
Construction and testing of Yarrowia lipolytica recombinant protein expression chassis cells based on the high-throughput screening and secretome.
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 4 papers.
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Who cites it
4 citing papers in PubMed, 8 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
- Omics-Based Expression Cassette for Heterologous Protein Production inACS synthetic biology · 2026Article
- Machine learning-assisted rational design and evolution of novel signal peptides inSynthetic and systems biotechnology · 2025Article
- 'Small volume-big problem': culturing Yarrowia lipolytica in high-throughput micro-formats.Microbial cell factories · 2024Review
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Authors and funding
6 authors at 4 institutions in 2 countries.
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Abstract
backgroundIn the recombinant protein market with broad economic value, the rapid development of synthetic biology has made it necessary to construct an efficient exocrine expression system for the different heterologous proteins. Yarrowia lipolytica possesses unique advantages in nascent protein transport and glycosylation modification, so it can serve as a potential protein expression platform. Although the Po1 series derived from W29 is often used for the expression of the various heterologous proteins, the ability of W29 to secrete proteins has not been verified and the Po1 series has been found to be not convenient for further gene editing.
resultsA total of 246 Y. lipolytica strains were evaluated for their secretory capacity through performing high-throughput screening in 48-well plate. Thereafter, following two rounds of shake flask re-screening, a high-secreting protein starting strain DBVPG 5851 was obtained. Subsequently, combined with the extracellular protein types and relative abundance information provided by the secretome of the starting strain, available chassis cell for heterologous protein expression were preliminarily constructed, and it was observed that the most potential signal peptide was derived from YALI0D20680g.
conclusionsThis study offers a novel perspective on the diversification of Y. lipolytica host cells for the heterologous protein expression and provides significant basis for expanding the selection space of signal peptide tools in the future research.
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