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Protein Science (2008), 17:606-613. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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The epitope space of the human proteome

Lisa Berglund1, Jorge Andrade1, Jacob Odeberg, and Mathias Uhlén

School of Biotechnology, AlbaNova University Center, Royal Institute of Technology, SE-106 91 Stockholm, Sweden

(RECEIVED November 8, 2007; FINAL REVISION December 22, 2007; ACCEPTED December 27, 2007)

In the post-genome era, there is a great need for protein-specific affinity reagents to explore the human proteome. Antibodies are suitable as reagents, but generation of antibodies with low cross-reactivity to other human proteins requires careful selection of antigens. Here we show the results from a proteome-wide effort to map linear epitopes based on uniqueness relative to the entire human proteome. The analysis was based on a sliding window sequence similarity search using short windows (8, 10, and 12 amino acid residues). A comparison of exact string matching (Hamming distance) and a heuristic method (BLAST) was performed, showing that the heuristic method combined with a grid strategy allows for whole proteome analysis with high accuracy and feasible run times. The analysis shows that it is possible to find unique antigens for a majority of the human proteins, with relatively strict rules involving low sequence identity of the possible linear epitopes. The implications for human antibody-based proteomics efforts are discussed.

Keywords: proteomics; antigen; epitope; sequence similarity; antibody; grid


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