Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C

Mona Pourjafar, Michaela Miehe, Rezvan Najafi, Meysam Soleimani*, Edzard Spillner

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Abstract

Minibodies (single-chain Fv-CH3) are fusion proteins of a single-chain variable fragment (scFv) to the human IgG1 CH3 domain. They exhibit superior properties as compared to whole antibodies due to their smaller size and less complex composition, and also as compared to scFvs due to the two antigen-binding domains, for immunotherapy and imaging of various carcinomas including breast cancer. In the current study, efficient production of the recombinant anti-MUC-1 minibody for its dominant format (VH-VL) was obtained in the periplasmic space of the Escherichia coli BL21 (DE3) expression system. The active recombinant protein was successfully purified from soluble fraction. Functional assays presented the in vitro targeting properties and specificity of the expressed anti-MUC-1 HL minibody in the MUC-1 positive cell lines compared to normal cell.

Original languageEnglish
Article number106148
JournalProtein Expression and Purification
Volume199
ISSN1046-5928
DOIs
Publication statusPublished - Nov 2022

Keywords

  • Breast cancer
  • Engineered antibody
  • Mammalian expression
  • Minibody
  • Mucin-1
  • Periplasmic expression

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