The cytotoxicity of Bacillus thuringiensis subsp. coreanensis A1519 strain against the human leukemic T cell

Biochim Biophys Acta. 2003 Jun 20;1622(1):29-35. doi: 10.1016/s0304-4165(03)00102-8.

Abstract

A novel cytotoxic protein was isolated from the crystal produced by Bacillus thuringiensis subsp. coreanensis A1519 strain. Upon treatment of the crystal proteins by proteinase K, the significant cytotoxicity toward the leukemic T cell, MOLT-4, was exhibited. The microscopic observation indicated that the cell death was accompanied by no extensive rupture of the cell membrane. It was, therefore, suggested that the cell death of MOLT-4 was induced through a mechanism other than the colloid-osmotic swelling and cell lysis as caused by hitherto known B. thuringiensis crystal proteins. The 29-kDa polypeptide proved to be an active component of the proteinase K-digested A1519 crystal proteins. EC(50) of the purified 29-kDa polypeptide was 0.078 microg/ml. The N-terminal amino acid sequence of the 29-kDa polypeptide shared no significant homology with all the known proteins, suggesting that this polypeptide belong to a new family of B. thuringiensis crystal proteins. In the ligand blotting analysis, specific binding proteins for the 29-kDa polypeptide were detected from the cell membrane of MOLT-4.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents / pharmacology*
  • Bacterial Proteins / analysis
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / pharmacology*
  • Bacterial Toxins*
  • Endotoxins / analysis
  • Endotoxins / metabolism
  • Endotoxins / pharmacology*
  • Hemolysin Proteins
  • Humans
  • Leukemia / drug therapy*
  • Membrane Proteins / metabolism
  • Molecular Weight
  • T-Lymphocytes / drug effects*
  • Tumor Cells, Cultured

Substances

  • Antineoplastic Agents
  • Bacterial Proteins
  • Bacterial Toxins
  • Endotoxins
  • Hemolysin Proteins
  • Membrane Proteins
  • insecticidal crystal protein, Bacillus Thuringiensis