ArticleCancer gene therapy2013
Expression of β-glucuronidase on the surface of bacteria enhances activation of glucuronide prodrugs.
Article in Cancer gene therapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Biodesulfurization and activation of a thionated levofloxacin derivative: antimicrobial evaluation and LC-MS-based metabolic profiling.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Developing a Virus-Binding Bacterium Expressing Mx Protein on the Bacterial Surface to Prevent Grouper Nervous Necrosis Virus Infection.Journal of microbiology and biotechnology · 2021Article
- Bacteria-Mediated Synergistic Cancer Therapy: Small Microbiome Has a Big Hope.Nano-micro letters · 2021Review
- Chemopreventive Effect of the Germinated Oat and its Phenolic-AVA Extract in Azoxymethane/Dextran Sulfate Sodium (AOM/DSS) Model of Colon Carcinogenesis in Mice.Foods (Basel, Switzerland) · 2020Article
- Poly-protein G-expressing bacteria enhance the sensitivity of immunoassays.Scientific reports · 2017Article
- Escherichia coli surface display of single-chain antibody VRC01 against HIV-1 infection.Virology · 2015Article
- Impediments to enhancement of CPT-11 anticancer activity by E. coli directed beta-glucuronidase therapy.PloS one · 2015Article
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Authors and funding
12 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Extracellular activation of hydrophilic glucuronide prodrugs by β-glucuronidase (βG) was examined to increase the therapeutic efficacy of bacteria-directed enzyme prodrug therapy (BDEPT). βG was expressed on the surface of Escherichia coli by fusion to either the bacterial autotransporter protein Adhesin (membrane βG (mβG)/AIDA) or the lipoprotein (lpp) outermembrane protein A (mβG/lpp). Both mβG/AIDA and mβG/lpp were expressed on the bacterial surface, but only mβG/AIDA displayed enzymatic activity. The rate of substrate hydrolysis by mβG/AIDA-BL21cells was 2.6-fold greater than by pβG-BL21 cells, which express periplasmic βG. Human colon cancer HCT116 cells that were incubated with mβG/AIDA-BL21 bacteria were sensitive to a glucuronide prodrug (p-hydroxy aniline mustard β-D-glucuronide, HAMG) with an half maximal inhibitory concentration (IC50) value of 226.53±45.4 μM, similar to the IC50 value of the active drug (p-hydroxy aniline mustard, pHAM; 70.6±6.75 μM), indicating that mβG/AIDA on BL21 bacteria could rapidly and efficiently convert HAMG to an active anticancer agent. These results suggest that surface display of functional βG on bacteria can enhance the hydrolysis of glucuronide prodrugs and may increase the effectiveness of BDEPT.
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