Increased yield and activity of soluble single-chain antibody fragments by combining high-level expression and the Skp periplasmic chaperonin

Chris Mavrangelos, Michael Thiel, Penelope J. Adamson, Debbrah J. Millard, Silvia Nobbs, Heddy Zola, Ian C. Nicholson

Research output: Contribution to journalArticle

36 Citations (Scopus)


The success of recombinant antibody fragments as diagnostic reagents and therapeutic agents depends on the availability of sufficient functional material. We have produced a bacterial expression vector that combines high-level expression driven by a modified Shine-Dalgarno sequence with the periplasmic chaperonin Skp. Using this vector, we are able to obtain higher yields of soluble antibody fragments from cultures without the need for supplementation of the culture medium during expression. The fragments produced in the presence of the Skp show improved antigen binding activity compared to when the chaperonin is absent.

Original languageEnglish
Pages (from-to)289-295
Number of pages7
JournalProtein Expression and Purification
Issue number2
Publication statusPublished - 1 Jan 2001


  • Periplasmic chaperonin
  • Protein expression
  • Single-chain antibody fragment

ASJC Scopus subject areas

  • Biotechnology

Cite this