Intracellular expression of the anti-erbB-2 sFv N29 fails to accomplish efficient target modulation

Jon E. Grim, Gene P. Siegal, Ronald D. Alvarez, David T. Curiel

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


The use of intracellular single chain antibodies has recently emerged as a highly efficient method of downregulating or ablating protein expression. In this regard, we have demonstrated that a single chain antibody directed against the extracellular domain of the erbB-2 molecule causes a specific toxicity in erbB-2 positive tumor types. To further investigate the mechanism of this effect, we developed a second anti-erbB-2 sFv predicted to recognize an alternate extracellular epitope of the erbB-2 molecule. When produced as a secreted protein from the erbB-2 negative COS-1 cell line, this sFv binds specifically to erbB-2 positive cells, indicating that cellular machinery is able to produce a properly folded and functional sFv protein. However, by several assays, this sFv was shown to be unable to retain the erbB-2 protein within the ER. These negative results have implications for the evaluation and utilization of sFv knockout strategies in experimental contexts.

Original languageEnglish
Pages (from-to)699-703
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Sep 29 1998


  • ErbB-2
  • Intrabody
  • Single chain antibody (sFv)


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