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Transport of heterologous proteins to the periplasmic space of Pseudomonas fluorescens using a variety of native signal sequences


Bacterial expression of recombinant proteins containing disulfide bonds is facilitated by transport of the proteins to the periplasmic space. Several Pseudomonas fluorescens signal sequences have been identified that efficiently direct proteins to the periplasm and provide solubility and yield advantages over the production of proteins fused to the PelB signal sequence in E. coli. For a single chain antibody fragment, the final yield varied from about 1 g/l to 10 g/l when expression in P. fluorescens involved fusion to various P. fluorescens signal sequences.

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The authors would like to acknowledge the excellent technical assistance of Barbara Morach, Angel Salazar, Fareed Sajan, Michael Donahue, Tracey Thomas, Deborah Mun and Ping Xu. The authors would also like to thank Paul Roessler for critical review of the manuscript.

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Correspondence to Diane M. Retallack.

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Retallack, D.M., Schneider, J.C., Mitchell, J. et al. Transport of heterologous proteins to the periplasmic space of Pseudomonas fluorescens using a variety of native signal sequences. Biotechnol Lett 29, 1483–1491 (2007).

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  • Signal sequence
  • Secretion
  • Recombinant protein expression