Influence of growth temperature on the production of antibody Fab fragments in different microbes: A host comparative analysis
Abstract
Microorganisms encounter diverse stress conditions in their native habitats but also during fermentation processes, which have an impact on industrial process performance. These environmental stresses and the physiological reactions they trigger, including changes in the protein folding/secretion machinery, are highly interrelated. Thus, the investigation of environmental factors, which influence protein expression and secretion is still of great importance. Among all the possible stresses, temperature appears particularly important for bioreactor cultivation of recombinant hosts, as reductions of growth temperature have been reported to increase recombinant protein production in various host organisms. Therefore, the impact of temperature on the secretion of proteins with therapeutic interest, exemplified by a model antibody Fab fragment, was analyzed in five different microbial protein production hosts growing under steady-state conditions in carbon-limited chemostat cultivations. Secretory expression of the heterodimeric antibody Fab fragment was successful in all five microbial host systems, namely Saccharomyces cerevisiae, Pichia pastoris, Trichoderma reesei, Escherichia coli and Pseudoalteromonas haloplanktis. In this comparative analysis we show that a reduction of cultivation temperature during growth at constant growth rate had a positive effect on Fab 3H6 production in three of four analyzed microorganisms, indicating common physiological responses, which favor reco…
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Several studies have demonstrated that yield of recombinant antibody fragments in E. coli significantly improves at growth temperature below 30 °C, likely due to reduction of translation rate that favors proper Ig-like folding and reduces aggregation.
“Several studies have demonstrated that the yield of recombinant antibody fragments in E. coli significantly improves at growth temperature below 30 °C, likely due to the reduction of translation rate that favors proper Ig-like folding and reduces aggregation [90,91,92].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [91]
Cites
van Dijken, J. P., Bauer, J., Brambilla, L., Duboc, P., Francois, J. M., Gancedo, C., Giuseppin, M. L. F., Heijnen, J. J., Hoare, M., Lange, H. C., et al. (2000) · Enzyme and Microbial Technology · doi:10.1016/s0141-0229(00)00162-9 · Cited by 598 · see citing works
Self-citationKasemets, K., Nisamedtinov, I., Laht, T.-M., Abner, K., & Paalme, T. (2007) · Antonie van Leeuwenhoek · doi:10.1007/s10482-007-9141-y · Cited by 34 · see citing works
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Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments
Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works
Corchero, J. L., Gasser, B., Resina, D., Smith, W., Parrilli, E., Vázquez, F., Abasolo, I., Giuliani, M., Jäntti, J., Ferrer, P., et al. (2013) · Biotechnology Advances · doi:10.1016/j.biotechadv.2012.09.001 · Cited by 133 · see citing works
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- Authors
- Dragosits, M., Frascotti, G., Bernard‐Granger, L., Vázquez, F., Giuliani, M., Baumann, K., Rodríguez‐Carmona, E., Tokkanen, J., Parrilli, E., Wiebe, M. G., Kunert, R., Maurer, M., Gasser, B., Sauer, M., Branduardi, P., Pakula, T., Saloheimo, M., Penttilä, M., Ferrer, P., Luisa Tutino, M., Villaverde, A., Porro, D., & Mattanovich, D.
- Affiliations
- BOKU University (AT)
- University of Milano-Bicocca (IT)
- VTT Technical Research Centre of Finland (FI)
- Universitat Autònoma de Barcelona (ES)
- University of Naples Federico II (IT)
- Hochschule Campus Wien (AT)
- Corresponding author
- Mattanovich, Diethard
- ORCID
- Venue
- Biotechnology Progress
- Publisher
- Wiley
- Published
- 2010-12-23
- Volume
- 27
- Issue
- 1
- Pages
- 38-46
- ISSN
- 1520-6033 (ISSN-L)
- 8756-7938
- OpenAlex
- W1966308881
- Cited by
- 59
- References
- 2
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 4 · 2023: 7 · 2022: 5 · 2021: 1 · 2020: 2 · 2019: 4 · 2018: 3 · 2017: 6 · 2016: 5 · 2015: 2 · 2014: 7 · 2013: 3 · 2012: 2
- FWCI
- 1.04
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Biotechnology Progress (publishedVersion)
- PubMed (publishedVersion)
- BOA (University of Milano-Bicocca) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- growth temperature, antibody Fab fragment, recombinant protein secretion, Saccharomyces cerevisiae, Pichia pastoris, Trichoderma reesei, Escherichia coli, Pseudoalteromonas haloplanktis, chemostat cultivation, environmental stress
- MeSH terms
- Bacteria, Enzyme-Linked Immunosorbent Assay, Immunoglobulin Fab Fragments, Species Specificity, Temperature, Yeasts
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