The heavy chain of tetanus toxin can mediate the entry of cytotoxic gelonin into intact cells

FEBS Letters

Morrice, Lora M.¹  Johnstone, Stephen R.¹  van Heyningen, Simon¹ 

[1] Department of Biochemistry, University of Edinburgh, Hugh Robson Building, George Square, Edinburgh EH8 9XD, UK

关键词: Tetanus toxin;    Gelonin;    Internalization;    HT29 cell;    DMSO;    dimethyl sulphoxide;    MTT;    3-(4;    5-dimethylthiazol-2-yl)-2;    5-diphenyltetrazolium blue;    PBS;    10 mM sodium phosphate;    0.9% sodium chloride;    pH 7.2;    PDP-;    pyridyldithiopropionyl-;    SDS;    sodium dodecylsulphate;    SPDP;    N- succinimidyl-3-(2-pyridyldithio)propionate;    TCA;    trichloroacetic acid;   

DOI  :  10.1016/0014-5793(90)80893-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An artificial conjugate of the heavy chain of tetanus toxin linked by a disulphide bond to the impermeant ribosome-inactivating protein gelonin is cytotoxic to intact HT29 cells by inhibiting intracellular protein synthesis. Neither toxin nor gelonin alone has any significant effect. This shows that the heavy chain has the ability to mediate internalization of a protein to which it is bound by a disulphide bond. Thus the normal role of the tetanus toxin heavy chain may be to allow entry of the light chain into a cell.

【 授权许可】

Unknown