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Receptor-mediated endocytosis as a selection force to enrich bacteria expressing rhodostomin on their surface

J Biomed Sci. 2000 Jan-Feb;7(1):42-50. doi: 10.1007/BF02255917.

Abstract

Previously, we developed a TraT display system to express snake venom rhodostomin (RHO), a disintegrin, on the external surface of Escherichia coli [J Biomed Sci 6:64-70;1999]. To show a new potential use of the TraT display system, we employed a biotin labeling technique coupled with SDS-PAGE and flow cytometry analyses to further demonstrate and confirm the expression of TraT-RHO on the E. coli surface. We also showed that the expression of TraT-RHO on the cell surface not only facilitated the bacteria adhesion to BHK-21 cells but also induced bacterial internalization into BHK-21 cells. This feature allowed us to enrich the TraT-RHO expression bacteria about 10,000-fold starting with a mixture of TraT-RHO bacteria with beta-galactosidase-positive bacteria in a ratio of 10(2):10(7) through four cycles of BHK-21 cell endocytosis and replating of engulfed bacteria on agar plates. We therefore suggest that the TraT display system can be applied to select out bacteria expressing a specific peptide sequence from a large population of display library through the process of receptor-mediated endocytosis and reamplification cycles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Line / metabolism
  • Cloning, Molecular / methods*
  • Cricetinae
  • Endocytosis / drug effects*
  • Escherichia coli / chemistry
  • Escherichia coli / genetics
  • Flow Cytometry
  • Fluorescent Antibody Technique
  • Gene Expression
  • Membrane Proteins / biosynthesis
  • Mesocricetus
  • Peptide Library
  • Peptides / metabolism*
  • Phenotype
  • Platelet Aggregation Inhibitors / metabolism*
  • Receptors, Cell Surface / physiology*
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism

Substances

  • Membrane Proteins
  • Peptide Library
  • Peptides
  • Platelet Aggregation Inhibitors
  • Receptors, Cell Surface
  • Recombinant Fusion Proteins
  • rhodostomin