ArticleCurrent microbiology2008
Construction of a novel Pichia pastoris cell-surface display system based on the cell wall protein Pir1.
Article in Current microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 25 citations in OpenAlex.
- Biofilm-Based Biocatalysis for Galactooligosaccharides Production by the Surface Display of β-Galactosidase inInternational journal of molecular sciences · 2023Article
- Homogeneous production and characterization of recombinant N-GlcNAc-protein in Pichia pastoris.Microbial cell factories · 2020Article
- Cell-Surface Displayed Expression of Trehalose Synthase fromFrontiers in microbiology · 2017Article
- Arming Technology in Yeast-Novel Strategy for Whole-cell Biocatalyst and Protein Engineering.Biomolecules · 2013Article
- Development of a novel rDNA based plasmid for enhanced cell surface display on Yarrowia lipolytica.AMB Express · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel system based on Pir1 from Saccharomyces cerevisiae was developed for cell-surface display of heterologous proteins in Pichia pastoris with the alpha-factor secretion signal sequence. As a model protein, enhanced green fluorescence protein (EGFP) was fused to the N-terminal of the mature peptide of Pir1 (Pir1-a). The expression of fusion protein EGFP-Pir1-a was irregular throughout the P. pastoris cell surface per detection by confocal laser scanning microscopy. A truncated sequence containing only the internal repetitive sequences of Pir1-a (Pir1-b) was used as a new anchor protein in further study. The fusion protein EGFP-Pir1-b was expressed uniformly on the cell surface. The fluorescence intensity of the whole yeast was measured by spectrofluorometer. Western blot confirmed that the fusion proteins were released from cell walls after mild alkaline treatment. The results indicate that a Pir1-based system can express proteins on the surface of P. pastoris and that the fusion proteins do not affect the manner in which Pir1 attaches to the cell wall. The repetitive sequences of Pir1 are required for cell wall retention, and the C-terminal sequence contributes to the irregular distribution of fusion proteins in P. pastoris.
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