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Originally published In Press as doi:10.1074/mcp.M500239-MCP200 on October 31, 2005.
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Molecular & Cellular Proteomics 5:245-255, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

A Novel Subtractive Antibody Phage Display Method to Discover Disease Markers*

Daniëlle Hof{ddagger}, Kalok Cheung{ddagger}, Hilde E. Roossien{ddagger}, Ger J. M. Pruijn{ddagger} and Jos M. H. Raats{ddagger},§,¶

From the {ddagger} Department of Biochemistry, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen, NL-6500 HB Nijmegen, The Netherlands and § ModiQuest B. V., NL-6525 GA Nijmegen, The Netherlands

Today’s research demands fast identification of potential diagnostic and therapeutic targets. We describe a novel phage display strategy to identify disease-related proteins that are specifically expressed in a certain (diseased) tissue or cells. Phages displaying antibody fragments are selected on complex protein mixtures in a two-step manner combining subtractive selection in solution with further enrichment of specific phages on two-dimensional Western blots. Targets recognized by the resulting recombinant antibodies are immunoaffinity-purified and identified by mass spectrometry. We used antibody fragment libraries from autoimmune patients to discover apoptosis-specific and disease-related targets. One of the three identified targets is the U1-70K protein, a marker for systemic lupus erythematosus overlap disease. Interestingly the epitope on U1-70K recognized by the selected recombinant antibody was shown to be apoptosis-dependent, and such epitopes are believed to be involved in breaking tolerance to self-antigens. The other two proteins were identified as polypyrimidine tract-binding protein-associated splicing factor (PSF)/nuclear RNA- and DNA-binding protein of 54 kDa (p54nrb) and heterogeneous ribonucleoprotein C.

To whom correspondence should be addressed: Dept. of Biochemistry 161, Radboud University Nijmegen, P. O. Box 9101, NL-6500 HB Nijmegen, The Netherlands. Tel.: 31-24-3614253; Fax: 31-24-3540525; E-mail: j.raats{at}ncmls.ru.nl


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This article has been cited by other articles:


Home page
 Brief Funct Genomic ProteomicHome page
D. Saerens, G. H. Ghassabeh, and S. Muyldermans
Antibody technology in proteomics
Brief Funct Genomic Proteomic, July 1, 2008; 7(4): 275 - 282.
[Abstract] [Full Text] [PDF]


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