Source:http://linkedlifedata.com/resource/pubmed/id/20138085
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
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| pubmed:dateCreated |
2010-5-10
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| pubmed:abstractText |
The immunogenic properties of chimeric potato virus X (PVX) particles engineered to display the synthetic R9 peptide have been evaluated. The R9 peptide is a consensus sequence derived from diverse variants of the hypervariable region 1 from the hepatitis C virus (HCV) envelope protein E2. Two different constructs were designed, with the R9 peptide expressed either as an indirect fusion via the ribosomal skip 2A (PVX(R9-2A)CP) sequence or as a direct PVX coat protein fusion (PVX(R9)CP). Systemic infection of Nicotiana benthamiana plants was only achieved with PVX(R9-2A)CP constructs, and the presence of the R9 peptide was detected in extracts from these plants by ELISA, Western blot and electron microscopy using specific anti-R9 antibodies. The virus particles were recovered at yields of up to 125mg/kg from leaf material. BALB/c mice immunized with purified PVX(R9-2A)CP particles developed specific anti-R9 IgG titers of up to 1:50,000. Monoclonal anti-R9 antibodies were obtained from the spleen of a mouse immunized with PVX(R9-2A)CP particles and characterized by Western blot and electron microscopy. Sera from patients infected chronically with HCV were found to react specifically with PVX(R9-2A)CP particles in 35% of cases.
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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, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Complementarity Determining Regions,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatitis C Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Hepatitis Vaccines,
http://linkedlifedata.com/resource/pubmed/chemical/glycoprotein E2, Hepatitis C virus
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
1879-0984
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2010 Elsevier B.V. All rights reserved.
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| pubmed:issnType |
Electronic
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| pubmed:volume |
166
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
12-20
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| pubmed:meshHeading |
pubmed-meshheading:20138085-Animals,
pubmed-meshheading:20138085-Antibodies, Monoclonal,
pubmed-meshheading:20138085-Complementarity Determining Regions,
pubmed-meshheading:20138085-Female,
pubmed-meshheading:20138085-Genetic Vectors,
pubmed-meshheading:20138085-Hepacivirus,
pubmed-meshheading:20138085-Hepatitis C Antibodies,
pubmed-meshheading:20138085-Humans,
pubmed-meshheading:20138085-Immunoglobulin G,
pubmed-meshheading:20138085-Mice,
pubmed-meshheading:20138085-Mice, Inbred BALB C,
pubmed-meshheading:20138085-Microscopy, Electron,
pubmed-meshheading:20138085-Potexvirus,
pubmed-meshheading:20138085-Recombination, Genetic,
pubmed-meshheading:20138085-Tobacco,
pubmed-meshheading:20138085-Viral Envelope Proteins,
pubmed-meshheading:20138085-Viral Hepatitis Vaccines,
pubmed-meshheading:20138085-Virion
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| pubmed:year |
2010
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| pubmed:articleTitle |
Immunogenic properties of chimeric potato virus X particles displaying the hepatitis C virus hypervariable region I peptide R9.
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| pubmed:affiliation |
Institute for Molecular Biotechnology (Biology VII), RWTH Aachen University, Worringerweg 1, 52074 Aachen, Germany.
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| pubmed:publicationType |
Journal Article
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