Reference - Detail
| RRC ID | 43875 |
|---|---|
| Author | Tabata A, Ohkubo Y, Sakakura E, Tomoyasu T, Ohkura K, Nagamune H. |
| Title | Investigation of a bacterial pore-forming chimera toxin for application as a novel drug-delivery system tool. |
| Journal | Anticancer Res |
| Abstract |
BACKGROUND/AIM:Cholesterol-dependent cytolysins (CDCs) are pore-forming toxins from Gram-positive bacteria. The aim of this study was to investigate the potential of a CDC, intermedilysin, as a drug-delivery system (DDS) for clinical application. MATERIALS AND METHODS:Intermedilysin was modified by the addition of a disulfide bridge to regulate pore formation, by swapping domain 4 to provide cholesterol-binding capacity, and by the introduction of a targeting domain. The resultant chimera protein, His-LTBP-CDC(ss)(IP), was investigated for its use as a DDS tool in vitro. RESULTS:His-LTBP-CDC(ss)(IP) exhibited a regulated pore-forming capacity under reducing conditions. This chimera protein was able to deliver a drug-carrier liposome specifically to the target cell, to be endocytosed into the cell with subsequent release of the components into the cytoplasm. CONCLUSION:A chimera protein derived from the bacterial pore-forming toxin intermedilysin (His-LTBP-CDC(ss)(IP)) forms the basis for a novel DDS tool. |
| Volume | 32(6) |
| Pages | 2323-9 |
| Published | 2012-6-1 |
| PII | 32/6/2323 |
| PMID | 22641669 |
| MeSH | Bacteriocins / administration & dosage* Bacteriocins / chemical synthesis Cell Line, Tumor Drug Delivery Systems / methods* Electrophoresis, Polyacrylamide Gel Humans Liposomes Microscopy, Fluorescence Recombinant Fusion Proteins / administration & dosage* Recombinant Fusion Proteins / chemical synthesis |
| IF | 1.994 |
| Times Cited | 6 |
| WOS Category | ONCOLOGY |
| Resource | |
| Human and Animal Cells | NB1RGB(RCB0222) A549(RCB0098) |