rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
2008-4-21
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pubmed:abstractText |
Matrix protein 2 (M2) of influenza A is a tetrameric type III membrane protein that functions as a proton-selective channel. The extracellular domain (M2e) has remained nearly invariable since the first human influenza strain was isolated in 1933. By linking a modified form of the leucine zipper of the yeast transcription factor GCN4 to M2e, we obtained a recombinant tetrameric protein, M2e-tGCN4. This protein mimics the quaternary structure of the ectodomain of the natural M2 protein. M2e-tGCN4 was purified, biochemically characterized, and used to immunize BALB/c mice. High M2e-specific serum IgG antibody titers were obtained following either intraperitoneal or intranasal administration. Immunized mice were protected fully against a potentially lethal influenza A virus challenge. Antibodies raised by M2e-tGCN4 immunization specifically bound to the surface of influenza-infected cells and to an M2-expressing cell line. Using a M2e peptide competition enzyme-linked immunosorbent assay with M2-expressing cells as target, we obtained evidence that M2e-tGCN4 induces antibodies that are specific for the native tetrameric M2 ectodomain. Therefore, fusion of an oligomerization domain to the extracellular part of a transmembrane protein allows it to mimic the natural quaternary structure and can promote the induction of oligomer-specific antibodies.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18252707-10502819,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18252707-10520648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18252707-12628550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18252707-12744898,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18252707-1989386,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18252707-8782356
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11382-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18252707-Animals,
pubmed-meshheading:18252707-Chromatography, Gel,
pubmed-meshheading:18252707-Dose-Response Relationship, Drug,
pubmed-meshheading:18252707-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:18252707-Epitopes,
pubmed-meshheading:18252707-Immunoglobulin G,
pubmed-meshheading:18252707-Influenza Vaccines,
pubmed-meshheading:18252707-Mass Spectrometry,
pubmed-meshheading:18252707-Mice,
pubmed-meshheading:18252707-Mice, Inbred BALB C,
pubmed-meshheading:18252707-Models, Biological,
pubmed-meshheading:18252707-Molecular Conformation,
pubmed-meshheading:18252707-Peptides,
pubmed-meshheading:18252707-Protein Structure, Tertiary,
pubmed-meshheading:18252707-Viral Matrix Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
An influenza A vaccine based on tetrameric ectodomain of matrix protein 2.
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pubmed:affiliation |
Department of Molecular Biomedical Research, Vlaams Instituut voor Biotechnologie (VIB), B9052 Ghent, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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