Anchoring antibodies to membranes using a diphtheria toxin T domain‐ZZ fusion protein as a pH sensitive membrane anchor

FEBS Letters

Liger, Dominique¹  Nizard, Philippe¹  Gaillard, Carole¹  Gillet, Daniel¹ 

[1]Département d'Ingénierie et d'Etudes des Protéines (DIEP), DSV, CEA, CE Saclay, 91191 Gif-sur-Yvette Cedex, France

关键词: Diphtheria toxin;    Membrane anchor;    Membrane insertion;    Protein A;    Targeting;    Transmembrane domain;    FCCP;    carbonyl cyanide p-(trifluoromethoxy) phenylhydrazone;    lipo-ELIFA;    liposome enzyme linked immunofiltration assay;    LUV;    large unilamellar vesicles;    SUV;    small unilamellar vesicles;    T domain;    diphtheria toxin transmembrane domain;   

DOI  :  10.1016/S0014-5793(98)00890-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have constructed a fusion protein, T-ZZ, in which the IgG-Fc binding protein ZZ was fused to the C-terminus of the diphtheria toxin transmembrane domain (T domain). While soluble at neutral pH, T-ZZ retained the capacity of the T domain to bind to phospholipid membranes at acidic pH. Once anchored to the membrane, the ZZ part of the protein was capable of binding mouse monoclonal or rabbit polyclonal IgG. Our results show that the T-ZZ protein can function as a pH sensitive membrane anchor for the linkage of IgG to the membrane of lipid vesicles, adherent and non-adherent cells.

【 授权许可】

Unknown