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Engineering Saccharomyces boulardii for cell surface display of heterologous protein. | LitMetric

Engineering Saccharomyces boulardii for cell surface display of heterologous protein.

J Biotechnol

School of Food Science and Biotechnology, Kyungpook National University, Daegu 41566, South Korea; Research Institute of Tailored Food Technology, Kyungpook National University, Daegu 41566, South Korea. Electronic address:

Published: January 2025

AI Article Synopsis

  • - Saccharomyces boulardii and Saccharomyces cerevisiae are over 99% genetically similar but have different metabolic functions, with S. cerevisiae's cell surface display system being well-known while S. boulardii's is not fully characterized.
  • - This study built six genetically modified strains of S. boulardii to express the enhanced green fluorescent protein (Egfp) alongside various anchor proteins to visualize the cell surface display system.
  • - The research found that the Sed1 anchor protein yielded the highest fluorescence intensity and enabled the engineered strain to effectively degrade inulin within 72 hours, confirming the successful development of a cell surface display system for S. boulardii.

Article Abstract

Saccharomyces boulardii and Saccharomyces cerevisiae share over 99 % genetic similarity yet exhibit distinct metabolic traits. While the cell surface display system of S. cerevisiae is well-documented, the equivalent system in S. boulardii has yet to be fully characterized. This study investigates the cell surface display system of S. boulardii for the expression of a heterologous protein using different anchor proteins. Six strains expressing the enhanced green fluorescent protein (Egfp) and an anchor protein as a fusion protein were constructed to visualize the cell surface display system. Then a heterologous endo-inulinase protein was expressed with selected anchor proteins through fluorescence intensity comparison. Analysis by fluorescence microscopy revealed that the anchor protein Sed1 exhibited the highest fluorescence intensity. Furthermore, expressed selected anchor proteins and heterologous protein, endo-inulinase, the engineered strain could degrade and consume almost inulin in 72 h. Through endo-inulinase expression, we confirmed that not only Egfp but also heterologous protein is well expressed, and we successfully built an S. boulardii cell surface display system.

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Source
http://dx.doi.org/10.1016/j.jbiotec.2024.11.013DOI Listing

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