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Volume 270, Number 41, Issue of October 13, 1995 pp. 24078-24085
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
An Antibody Fragment from a Phage Display Library Competes for Ligand Binding to the Low Density Lipoprotein Receptor Family and Inhibits Rhinovirus Infection

(Received for publication, June 23, 1995)

Regina A. Hodits ,  Johannes Nimpf ,  Doris M. Pfistermueller,  Thomas Hiesberger ,  Wolfgang J. Schneider ,  Tristan J. Vaughan ,  Kevin S. Johnson ,  Markus Haumer ,  Ernst Kuechler,  Greg Winter ,  Dieter Blaas

Recently antibodies with a wide range of binding specificities have been isolated from large repertoires of antibody fragments displayed on filamentous phage, including those that are difficult to raise by immunization. We have used this approach to isolate an antibody fragment against chicken very low density lipoprotein (VLDL) receptor. It binds to the receptor with good affinity (K = 2 times 10^8M) as measured by plasmon surface resonance, and competes for binding of natural ligands (vitellogenin, VLDL, and receptor-associated protein). The antibody also binds to other members of the low density lipoprotein (LDL) receptor family including rat LDL receptor and human and rat low density lipoprotein receptor-related protein (LRP/alpha(2)MR), and it competes for binding of receptor-associated protein to LRP/alpha(2)MR. Moreover, the antibody fragment inhibits infection of human fibroblasts deficient in LDL-R but expressing LRP/alpha(2)MR by human rhinovirus. Binding of the antibody is abolished upon reduction of the receptors and is strictly Ca dependent. The phage antibody thus recognizes the ligand binding site(s) of several members of the LDL receptor family, in contrast to antibodies produced by hybridoma technology.



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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.