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Anchoring antibodies to membranes using a diphtheria toxin T domain‐ZZ fusion protein as a pH sensitive membrane anchor
Author(s) -
Nizard Philippe,
Liger Dominique,
Gaillard Carole,
Gillet Daniel
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00890-4
Subject(s) - diphtheria toxin , membrane , chemistry , polyclonal antibodies , fusion protein , transmembrane protein , membrane protein , microbiology and biotechnology , biophysics , biochemistry , toxin , antibody , biology , receptor , recombinant dna , gene , immunology
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.