rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
11
|
pubmed:dateCreated |
1998-12-7
|
pubmed:abstractText |
The tumour-associated antigen epithelial glycoprotein-2 (EGP-2) is a promising target for detection and treatment of a variety of human carcinomas. Antibodies to this antigen have been successfully used in patients for imaging of small-cell lung cancer and for adjuvant treatment of minimal residual disease of colon cancer. We describe here the isolation and complete characterization of high-affinity single-chain variable fragments (scFv) to the EGP-2 antigen. First, the binding kinetics of four murine whole antibodies directed to EGP-2 (17-1A, 323/A3, MOC-31 and MOC-161) were determined using surface plasmon resonance (SPR). The MOC-31 antibody has the lowest apparent off-rate, followed by MOC-161 and 323/A3. The V-genes of the two MOC hybridomas were cloned as scFv in a phage display vector and antigen-binding phage were selected by panning on recombinant antigen. The scFvs compete with the original hybridoma antibodies for binding to antigen and specifically bind to human carcinomas in immunohistochemistry. MOC-31 scFv has an off-rate which is better than those of the bivalent 17-1A and 323/A3 whole antibodies, providing it with an essential characteristic for tumour retention in vivo. The availability of these high-affinity anti-EGP-2 antibody fragments and of their encoding V-genes creates a variety of possibilities for their future use as tumour-targeting vehicles.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-1737342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-1748994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-1907718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-1908075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-286328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-3262566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-3492266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-3510721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-3744383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-7493381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-7521646,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-7671252,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/9836471-9537586
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0007-0920
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
78
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1407-16
|
pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9836471-Animals,
pubmed-meshheading:9836471-Antibodies, Monoclonal,
pubmed-meshheading:9836471-Antigens, Neoplasm,
pubmed-meshheading:9836471-Base Sequence,
pubmed-meshheading:9836471-Cell Adhesion Molecules,
pubmed-meshheading:9836471-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:9836471-Genes, Immunoglobulin,
pubmed-meshheading:9836471-Genetic Vectors,
pubmed-meshheading:9836471-Humans,
pubmed-meshheading:9836471-Immunoglobulin Fragments,
pubmed-meshheading:9836471-Immunoglobulin Variable Region,
pubmed-meshheading:9836471-Mice,
pubmed-meshheading:9836471-Molecular Sequence Data,
pubmed-meshheading:9836471-Tumor Markers, Biological
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pubmed:year |
1998
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pubmed:articleTitle |
High-affinity recombinant phage antibodies to the pan-carcinoma marker epithelial glycoprotein-2 for tumour targeting.
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pubmed:affiliation |
Department of Pathology, Maastricht University, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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