Applied Cellular Physiology and Metabolic Engineering

Influence of growth temperature on the production of antibody Fab fragments in different microbes: A host comparative analysis

  1. Martin Dragosits1,
  2. Gianni Frascotti2,†,
  3. Lise Bernard-Granger3,†,
  4. Felícitas Vázquez4,5,†,
  5. Maria Giuliani6,†,
  6. Kristin Baumann7,†,
  7. Escarlata Rodríguez-Carmona4,5,
  8. Jaana Tokkanen3,
  9. Ermenegilda Parrilli6,
  10. Marilyn G. Wiebe3,
  11. Renate Kunert1,
  12. Michael Maurer1,8,
  13. Brigitte Gasser1,
  14. Michael Sauer1,8,
  15. Paola Branduardi2,
  16. Tiina Pakula3,
  17. Markku Saloheimo3,
  18. Merja Penttilä3,
  19. Pau Ferrer7,
  20. Maria Luisa Tutino6,
  21. Antonio Villaverde4,5,
  22. Danilo Porro2,
  23. Diethard Mattanovich1,8,*

Article first published online: 23 DEC 2010

DOI: 10.1002/btpr.524

Issue

Biotechnology Progress

Biotechnology Progress

Volume 27, Issue 1, pages 38–46, January/February 2011

Additional Information

How to Cite

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. and Mattanovich, D. (2011), Influence of growth temperature on the production of antibody Fab fragments in different microbes: A host comparative analysis. Biotechnol Progress, 27: 38–46. doi: 10.1002/btpr.524

Author Information

  1. 1

    Dept. of Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria

  2. 2

    Dept. of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy

  3. 3

    VTT Technical Research Centre, Espoo, Finland

  4. 4

    Institut de Biotecnologia i de Biomedicina and Dept. of Genètica i de Microbiologia, Universitat Autònoma de Barcelona, Barcelona, Spain

  5. 5

    CIBER de Bioingeniería, Biomateriales y Nanomedicina (CIBER-BBN), Bellaterra, Barcelona 08193, Spain

  6. 6

    Dept. of Organic Chemistry and Biochemistry, Università di Napoli Federico II, Naples, Italy

  7. 7

    Dept. of Chemical Engineering, Escola Tècnica Superior d'Enginyeria, Universitat Autònoma de Barcelona, Barcelona, Spain

  8. 8

    School of Bioengineering, University of Applied Sciences FH-Campus, Wien, Austria

  1. †

    Martin Dragosits, Gianni Frascotti, Lise Bernard-Granger, Felícitas Vázquez, Maria Giuliani, and Kristin Baumann contributed equally to this study

*Dept. of Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria

  1. †

    Martin Dragosits, Gianni Frascotti, Lise Bernard-Granger, Felícitas Vázquez, Maria Giuliani, and Kristin Baumann contributed equally to this study

Publication History

  1. Issue published online: 10 FEB 2011
  2. Article first published online: 23 DEC 2010
  3. Accepted manuscript online: 27 OCT 2010 09:16AM EST
  4. Manuscript Revised: 28 SEP 2010
  5. Manuscript Received: 28 MAY 2010

Funded by

  • European Science Foundation (ESF, program EuroScope)
  • Austrian Science Fund (FWF). Grant Number: I37-B03
  • Austrian Research Promotion Agency (Program FHplus)
  • Spanish Program on Chemical Process Technologies. Grant Number: CTQ2007 - 60347/PPQ
  • Complementary Actions Plan supporting the ESF EuroScope program. Grant Number: BIO2005-23733-E
  • integrated action HU2005-0001 of the Spanish Ministry of Science and Innovation
  • Generalitat de Catalunya. Grant Number: 2009SG-108
  • Academy of Finland. Grant Number: 112391
  • F.A.R. 2008. Grant Number: 12-1-5140000-27
  • CIBER de Bioingenieria, Biomateriales y Nanomedicina
  • VI National R&D and i Plan 2008-2011
  • Iniciativa Ingenio 2010
  • Consolider Program
  • CIBER Actions and financed by the Instituto de Salud Carlos III with assistance from the European Regional Development Fund
Corrected by:

Erratum: Erratum

Vol. 28, Issue 4, 1114, Article first published online: 23 JUL 2012

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Keywords:

  • recombinant protein production;
  • chemostat;
  • Saccharomyces cerevisiae;
  • Pichia pastoris;
  • Trichoderma reesei;
  • Escherichia coli;
  • Pseudoalteromonas haloplanktis

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 recombinant protein production in prokaryotic as well as eukaryotic microbes. © 2010 American Institute of Chemical Engineers Biotechnol. Prog., 2011

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