Abstract
We describe the selection of single chain Fv fragments (scFv) against recombinant murine prion protein (mPrP) from a synthetic human antibody phage display library. Six different antibodies were isolated after three rounds of panning against full-length mPrP. All antibodies recognized a truncated form of mPrP containing residues (121-231). The amino acid sequence of the CDR3 of the scFv fragments has been determined. Five of the antibodies have been over-expressed, purified and their affinity for full-length mPrP determined by ELISA. The observed binding affinities vary from 30 nM to 2.7 microM.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence / genetics
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Animals
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Complementarity Determining Regions / genetics
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Complementarity Determining Regions / immunology
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Complementarity Determining Regions / isolation & purification*
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Enzyme-Linked Immunosorbent Assay
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Gene Library
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Humans
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Immunoglobulin Fragments / immunology*
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Immunoglobulin Fragments / isolation & purification*
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Mice
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Prions / genetics
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Prions / immunology*
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Recombinant Proteins / genetics
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Recombinant Proteins / immunology*
Substances
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Complementarity Determining Regions
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Immunoglobulin Fragments
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Prions
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Recombinant Proteins
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immunoglobulin Fv