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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2004-3-1
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pubmed:abstractText |
Membrane fusion has many potential applications in biotechnology. Here we show that antibody-targeted cell fusion can be achieved by engineering a fusogenic viral membrane glycoprotein complex. Three different single-chain antibodies were displayed at the extracellular C terminus of the measles hemagglutinin (H) protein, and combinations of point mutations were introduced to ablate its ability to trigger fusion through the native viral receptors CD46 and SLAM. When coexpressed with the measles fusion (F) protein, using plasmid cotransfection or bicistronic adenoviral vectors, the retargeted H proteins could mediate antibody-targeted cell fusion of receptor-negative or receptor-positive index cells with receptor-positive target cells. Adenoviral expression vectors mediating human epidermal growth factor receptor (EGFR)-targeted cell fusion were potently cytotoxic against EGFR-positive tumor cell lines and showed superior antitumor potency against EGFR-positive tumor xenografts as compared with control adenoviruses expressing native (untargeted) or CD38-targeted H proteins.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigen-Antibody Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD46,
http://linkedlifedata.com/resource/pubmed/chemical/CD150 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/CD46 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Mcp protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1087-0156
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
331-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:14990955-Animals,
pubmed-meshheading:14990955-Antigen-Antibody Complex,
pubmed-meshheading:14990955-Antigens, CD,
pubmed-meshheading:14990955-Antigens, CD46,
pubmed-meshheading:14990955-Cell Line, Tumor,
pubmed-meshheading:14990955-Cell Membrane,
pubmed-meshheading:14990955-Cells, Cultured,
pubmed-meshheading:14990955-Cercopithecus aethiops,
pubmed-meshheading:14990955-Drug Delivery Systems,
pubmed-meshheading:14990955-Female,
pubmed-meshheading:14990955-Glycoproteins,
pubmed-meshheading:14990955-Humans,
pubmed-meshheading:14990955-Immunoglobulins,
pubmed-meshheading:14990955-Membrane Fusion,
pubmed-meshheading:14990955-Membrane Glycoproteins,
pubmed-meshheading:14990955-Mice,
pubmed-meshheading:14990955-Mice, Nude,
pubmed-meshheading:14990955-Neoplasms,
pubmed-meshheading:14990955-Protein Engineering,
pubmed-meshheading:14990955-Receptors, Cell Surface,
pubmed-meshheading:14990955-Recombinant Proteins,
pubmed-meshheading:14990955-Treatment Outcome,
pubmed-meshheading:14990955-Vero Cells
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pubmed:year |
2004
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pubmed:articleTitle |
Antibody-targeted cell fusion.
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pubmed:affiliation |
Molecular Medicine Program, Mayo Foundation, 200 First St. SW, Rochester, Minnesota 55905, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Evaluation Studies
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