Cited by 176Fungal and yeast genetics researchYeasts and Rust Fungi StudiesMicrobial Metabolic Engineering and Bioproduction

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Applications of yeast in biotechnology: protein production and genetic analysis

Cereghino, Geoffrey P Lin, Cregg, James M·1999·Current Opinion in Biotechnology

DOI 10.1016/s0958-1669(99)00004-x

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Abstract

Improvements in yeast expression systems, coupled with the development of yeast surface display and refinements in two-hybrid methodology, are expanding the role of yeasts in the process of understanding and engineering eukaryotic proteins.

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Lin Cereghino, 1999, Expression of heterologous proteins in the methylotrophic yeast Pichia pastoris, FEMS Microbiol Rev

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Background
Bothrops pauloensis Snake Venom Toxins: The Search for New Therapeutic Models
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“Among the most studied systems, heterologous expression in Pichia pastoris has been used as a molecular biology tool due to its ability to perform posttranslational modifications [156], a characteristic important to enzymatic, biological and clinical activities.”
Background
Improving the Secretory Production of the Heterologous Protein in Pichia pastoris by Focusing on Protein Folding
Yu, P., Zhu, Q., Chen, K., & Lv, X. (2014) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-014-1292-5 · Cited by 29
“been a major strategy for the genetic improvement of endoplasmic reticulum resident proteins [25, 32–34].”
Background
Development of an industrial medium and a novel fed-batch strategy for high-level expression of recombinant β-mananase by Pichia pastoris
Zheng, J. M., Zhao, W. L., Guo, N., Lin, F.-L., Tian, J., Wu, L., & Zhou, H. (2012) · Bioresource Technology · doi:10.1016/j.biortech.2012.05.065 · Cited by 28
“Furthermore, there is a fire hazard using methanol as an inducer and it is inappropriate for the production of foods and drugs (Cereghino and Cregg, 1999).”
Background
A Novel Application for Low Frequency Electrochemical Impedance Spectroscopy as an Online Process Monitoring Tool for Viable Cell Concentrations
Slouka, C., Wurm, D. J., Brunauer, G., Welzl, A., Oliver Spadiut, A., Fleig, J., & Herwig, C. (2016) · Sensors · doi:10.3390/s16111900 · Cited by 31
An improved system for estradiol-dependent regulation of gene expression in yeast
Quintero, M., Maya‐Miles, D., Arévalo-Rodrı́guez, M., Cebolla, Á., & Chávez, S. (2007) · Microbial Cell Factories · doi:10.1186/1475-2859-6-10 · Cited by 28
Expressing Cloned Genes for Protein Production, Purification, and AnalysisPreprint
Kielkopf, C. L., Bauer, W. R., & Urbatsch, I. L. (2020) · Cold Spring Harbor Protocols · doi:10.1101/pdb.top102129 · Cited by 28
Applications of yeast in drug discovery
Ma, D. (2001) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8308-5_3 · Cited by 26
Optimising light conditions increases recombinant protein production in Chlamydomonas reinhardtii chloroplasts
Carrera-Pacheco, S. E., Hankamer, B. D., & Oey, M. (2018) · Algal Research · doi:10.1016/j.algal.2018.04.011 · Cited by 26
Development of a universal influenza vaccine using hemagglutinin stem protein produced from Pichia pastoris
Wang, S.-C., Liao, H.-Y., Zhang, J., Cheng, T.-J. R., & Wong, C. (2018) · Virology · doi:10.1016/j.virol.2018.10.005 · Cited by 26
Hd86, the Bm86 tick protein ortholog in Hyalomma scupense (syn. H. detritum): Expression in Pichia pastoris and analysis of nucleotides and amino acids sequences variations prior to vaccination trials
Saïd, M. B., Galaï, Y., Canales, M., Nijhof, A. M., Mhadhbi, M., Jedidi, M., de la Fuente, J., & Darghouth, M. A. (2011) · Veterinary Parasitology · doi:10.1016/j.vetpar.2011.07.049 · Cited by 25
Heterologous expression of codon optimized Trichoderma reesei Cel6A in Pichia pastoris
Sun, F. F., Bai, R., Yang, H., Wang, F., He, J., Wang, C., & Tu, M. (2016) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2016.07.004 · Cited by 23
Plasmodium Permeomics: Membrane Transport Proteins in the Malaria Parasite
Kirk, K., Martin, R. E., Bröer, S., Howitt, S. M., & Saliba, K. J. (2005) · Springer eBooks · doi:10.1007/3-540-29088-5_13 · Cited by 22
“The high levels of expression obtained from most standard yeast expression systems may overload the secretory pathway, reducing plasma membrane expression [ 15 , 44].”
Background
RETRACTED ARTICLE: High efficient expression of a functional humanized single-chain variable fragment (scFv) antibody against CD22 in Pichia pastoris
Zarei, N., Vaziri, B., Shokrgozar, M. A., Mahdian, R., Fazel, R., & Khalaj, V. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-6071-2 · Cited by 21
“Experiments were carried out in triplicate for the establishment of standard curves and in duplicate for clone analysis with the following program: 95 °C for 10 min as an initial denaturation, 40 cycles of 95 °C for 15 s, and 60 °C for 1 min.”
Influential
Retracted
Extraction and purification of hepatitis B virus-like M particles from a recombinant Saccharomyces cerevisiae strain using alumina powder
Hadiji-Abbès, N., Martin, M., Benzina, W., Karray, H., Gergely, C., Gargouri, A. F., & Mokdad‐Gargouri, R. (2012) · Journal of Virological Methods · doi:10.1016/j.jviromet.2012.09.023 · Cited by 21
Low-Frequency Electrochemical Impedance Spectroscopy as a Monitoring Tool for Yeast Growth in Industrial Brewing Processes
Slouka, C., Brunauer, G., Kopp, J., Strahammer, M., Fricke, J., Fleig, J., & Herwig, C. (2017) · Chemosensors · doi:10.3390/chemosensors5030024 · Cited by 21
Murine Factor H Co-Produced in Yeast With Protein Disulfide Isomerase Ameliorated C3 Dysregulation in Factor H-Deficient Mice
Kerr, H., Herbert, A. P., Makou, E., Abramczyk, D., Malik, T. H., Lomax-Browne, H. J., Yang, Y., Pappworth, I. Y., Denton, H., Richards, A., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.681098 · Cited by 17
Saccharomyces cerevisiae Ghosts Using the Sponge-Like Re-Reduced Protocol
Amara, A. A. A. F. (2015) · SOJ Biochemistry · doi:10.15226/2376-4589/2/1/00107 · Cited by 17
“Yeast is an eukaryotic microorganism which has some unique properties different from bacterial cells [2,8-10].”
Background
NMR Monitoring of Accumulation and Folding of 15N-Labeled Protein Overexpressed in Pichia pastoris
de Lamotte, F., Boze, H., Blanchard, C., Klein, C., Moulin, G., Gautier, M., & Delsuc, M. (2001) · Protein Expression and Purification · doi:10.1006/prep.2001.1435 · Cited by 17
Molecular cloning, sequencing, expression of Chinese sturgeon cystatin in yeast Pichia pastoris and its proteinase inhibitory activity
Bai, J., Ma, D., Haihua, L., Jian, Q., Ye, X., Luo, J., Xong, X., Li, Y., & Liang, X. (2006) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2006.02.023 · Cited by 16
Escherichia coli and Pichia pastoris : microbial cell-factory platform for full-length IgG production
Krishna, S., Jung, S. T., & Lee, E. Y. (2024) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2024.2342969 · Cited by 15
Using response surface methodology optimize culture conditions for human lactoferrin production in desert Chlorella
Wenlun, W., Wu, X., Tan, J., Zhu, L., Mou, Y., Zhang, D., & Gao, J. (2018) · Protein Expression and Purification · doi:10.1016/j.pep.2018.11.004 · Cited by 15
Proteins in a DNA world: expression systems for their study.
Reyes‐Ruiz, J. M., & Barrera-Saldaña, H. A. (2006) · PubMed · Cited by 15
Heterologous Expression of Biologically Active Porcine Lactoferrin in Pichia Pastoris Yeast
Pecorini, C., Savazzini, F., Martino, P. A., Fusi, E., Fogher, C., & Baldi, A. (2005) · Veterinary Research Communications · doi:10.1007/s11259-005-0086-1 · Cited by 15
“…GAP promoter provides a constitutive expression level, the regulatable AOX 1 promoter “switches off” foreign protein expression before induction, minimizing the selection of nonexpressing transformants during the growth phase and allowing tighter control of expression (Cereghino and Cregg, 1999).”
BackgroundInfluential
Comparative proteome analysis of Hansenula polymorpha DL1 and A16
Kim, Y., Han, K. Y., Lee, K., Heo, J., Kang, H. A., & Lee, J. (2004) · PROTEOMICS · doi:10.1002/pmic.200300739 · Cited by 14
Expression ofNeospora caninumNcSRS2 surface protein inPichia pastorisand its application for serodiagnosis ofNeosporainfection
Pinheiro, A. F., Borsuk, S., Berne, M. E. A., Pinto, L. D. S., Andreotti, R., Roos, T. B., Roloff, B. C., & Leite, F. P. L. (2013) · Pathogens and Global Health · doi:10.1179/2047773213y.0000000082 · Cited by 13
Overview of the Purification of Recombinant Proteins Produced inEscherichia coli
Wingfield, P. T. (2002) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps0601s30 · Cited by 13
“A yeast expression system may be a wise choice for proteins that form insoluble inclusions in bacteria, and for the production of membrane-associated proteins (Cereghino and Clegg, 1999; UNITS 5.6-5.8).”
BackgroundInfluential
Efficient production of nanobodies against urease activity ofHelicobacter pylori in Pichia pastoris
Pourasadi, S., Gargari, S. L. M., Rajabibazl, M., & Nazarian, S. (2017) · TURKISH JOURNAL OF MEDICAL SCIENCES · doi:10.3906/sag-1509-121 · Cited by 12
So you Need a Protein - A Guide to the Production of Recombinant Proteins
Jayaraj, R., & Smooker, P. M. (2009) · The Open Veterinary Science Journal · doi:10.2174/1874318800903010028 · Cited by 12
“coli, yeast has advantages such as ease of microbial growth and cultivation on inexpensive growth media, while adding the ability to perform many post-translational modifications such as O- or N- linked glycosylation, phosphorylation, disulphide bridge formation, proteolytic processing and folding in a eukaryotic syst…”
BackgroundInfluential
Expression of Macrobrachium rosenbergii lipopolysaccharide- and β-1,3-glucan-binding protein (LGBP) in Saccharomyces cerevisiae and evaluation of its immune function
Du, J., Zhu, H., Cao, C., & Ma, Y. (2018) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2018.07.045 · Cited by 12
Gelatin expression from an engineered Saccharomyces cerevisiae CUP1 promoter in Pichia pastoris
Williams, K. E., & Olsen, D. R. (2021) · Yeast · doi:10.1002/yea.3554 · Cited by 10
“…characterized eukaryotic expression system that lacks the extensive potentially immunogenic posttranslational modifications of other yeast such as Saccharomyces cerevisiae (Grinna & Tschopp, 1989; Cereghino & Cregg, 1999; Cregg et al., 2000; Cereghino & Cregg, 2000; Lin Cereghino et al., 2002).”
Background
Engineering IsPETase and Its Homologues: Advances in Enzyme Discovery and Host Optimisation
Ogunlusi, T. S., Ikoyo, S. S., Dadashipour, M., & Gao, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146797 · Cited by 9
“The methylotrophic yeast P. pastoris is widely recognised as a versatile workhorse for the production of heterologous proteins in industrial applications [76,77].”
Production of fluorescent and cytotoxic K28 killer toxin variants through high cell density fermentation of recombinant Pichia pastoris
Gießelmann, E., Becker, B., & Schmitt, M. (2017) · Microbial Cell Factories · doi:10.1186/s12934-017-0844-0 · Cited by 9
Production of recombinant Aedes albopictus akirin in Pichia pastoris using an aqueous two-phase semicontinuous fermentation process
Moreno-Cid, J. A., Canales, M., & de la Fuente, J. (2012) · Biochemical Engineering Journal · doi:10.1016/j.bej.2012.07.020 · Cited by 9
Wine science in the omics era: The impact of systems biology on the future of wine research
Rossouw, D., & Bauer, F. F. (2009) · South African Journal of Enology and Viticulture · doi:10.21548/30-2-1429 · Cited by 8

Authors: Cereghino, G. P. L., & Cregg, J. M.
Corresponding author: Cregg, James M
Venue: Current Opinion in Biotechnology
Publisher: Elsevier BV
Published: 1999-10
Volume: 10
Issue: 5
Pages: 422-427
ISSN: 0958-1669 (ISSN-L)
DOI: 10.1016/s0958-1669(99)00004-x
OpenAlex: W2124157676
Cited by: 176
References: 41
Citations by year: 2025: 3 · 2024: 1 · 2023: 7 · 2022: 3 · 2021: 5 · 2020: 8 · 2019: 3 · 2018: 6 · 2017: 5 · 2016: 8 · 2015: 3 · 2014: 9 · 2013: 9 · 2012: 10
FWCI: 0.53
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Current Opinion in Biotechnology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (7r01dk043698-09)
U.S. Public Health Service (ER20334)
National Institute of Diabetes and Digestive and Kidney Diseases (DK-43698)
National Institute of Environmental Health Sciences (ES05759, F32ES005759)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Immunology and Microbiology › Microbiology › Yeasts and Rust Fungi Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
Keywords: yeast, protein expression systems, yeast surface display, two-hybrid system, genetic analysis, recombinant protein expression
MeSH terms: Biotechnology, Pichia, Recombinant Proteins, Saccharomyces cerevisiae, Yeasts, Protein Engineering, Gene Expression Regulation, Fungal

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Applications of yeast in biotechnology: protein production and genetic analysis

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