Recombinant antibody-metallothionein: design and evaluation for radioimmunoimaging.
We have produced a chimeric antibody (Ab) in which metallothionein, a well-characterized biological chelator of metals, was genetically fused to the F(ab') domain of the S107 Ab heavy chain. Coexpression with the Ab light chain that conveys specificity for the synthetic antigen phosphocholine was achieved in plasmacytoma cells. Metal- and antigen-binding domains of the Ab-metallothionein hybrid function with normal avidity and specificity. Ab-metallothionein can be efficiently loaded with 99mTc and used to specifically bind phosphocholine-haptenated cells in vitro or to localize plasma-cell ascites tumors in mice. The approach offers potential advantages for producing radiolabeled Ab for targeted radiotherapy and diagnostic imaging.
Das
C
C
Department of Microbiology, University of Texas Southwestern Medical Center, Dallas 75235.
Kulkarni
P V
PV
Constantinescu
A
A
Antich
P
P
Blattner
F R
FR
Tucker
P W
PW
D000818:Animals; D006241:Haptens; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry*; D008668:Metallothionein / Q000737:chemistry*; D051379:Mice; D008807:Mice, Inbred BALB C; D010767:Phosphorylcholine / Q000737:chemistry; D011877:Radionuclide Imaging / Q000379:methods*; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D013667:Technetium / Q000378:metabolism; D014162:Transfection
D006241:Haptens; D007140:Immunoglobulin Fab Fragments; D011993:Recombinant Fusion Proteins; D010767:Phosphorylcholine; D013667:Technetium; D008668:Metallothionein