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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1992-12-1
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pubmed:abstractText |
Our initial results with a bovine papilloma virus (BPV) vector expression system indicated that we could produce significant amounts of Epstein-Barr virus (EBV) gp340/220 in the supernatant of a mouse fibroblast cell line. We have now extended these findings to show that the truncated version of gp340/220, where the membrane anchor sequence is deleted, is produced even after extended passage of the cells, at a level of approximately 1 mg/4 x 10(8) cells. A simple purification protocol using Sephacryl S300HR and gelatin agarose gives a product which is greater than 90% pure. This product is recognized by anti-gp340 monoclonal antibodies from five different epitope groups and induces antibody that recognizes the authentic gp340/220 and neutralizes EBV in vitro. The purified gp340/220 can be used in ELISA and stimulates the proliferation of T-cell clones specific for gp340/220. These characteristics, together with the fact that BPV-transformed lines have been utilized for the production of pharmaceuticals for use in humans, suggest that this gp340/220 is suitable as a source of antigen for vaccination to prevent EBV infection and related diseases.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/EBV-associated membrane antigen...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Matrix Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
0264-410X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
777-82
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1332270-Animals,
pubmed-meshheading:1332270-Antibodies, Viral,
pubmed-meshheading:1332270-Antigens, Viral,
pubmed-meshheading:1332270-Bovine papillomavirus 1,
pubmed-meshheading:1332270-Clone Cells,
pubmed-meshheading:1332270-Fibroblasts,
pubmed-meshheading:1332270-Gene Expression Regulation,
pubmed-meshheading:1332270-Genetic Vectors,
pubmed-meshheading:1332270-Lymphocyte Activation,
pubmed-meshheading:1332270-Membrane Proteins,
pubmed-meshheading:1332270-Mice,
pubmed-meshheading:1332270-Mice, Inbred BALB C,
pubmed-meshheading:1332270-T-Lymphocytes,
pubmed-meshheading:1332270-Viral Envelope Proteins,
pubmed-meshheading:1332270-Viral Matrix Proteins
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pubmed:year |
1992
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pubmed:articleTitle |
Purification and characterization of Epstein-Barr virus gp340/220 produced by a bovine papillomavirus virus expression vector system.
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pubmed:affiliation |
Department of Molecular Biology, Paterson Institute for Cancer Research, Manchester, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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