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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1998-6-1
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pubmed:abstractText |
A recombinant protein containing part of the dengue (DEN) 2 envelope protein was evaluated as a subunit immunogen for vaccination against DEN virus infection. A gene fragment encoding amino acids 298-400 (B domain) of the DEN-2 virus envelope was expressed as a fusion protein with the maltose binding protein (MBP) of Escherichia coli. This recombinant, DEN-2(B)/MBP, was purified and analyzed for its antigenicity, immunogenicity, and ability to protect mice against lethal challenge. The recombinant antigen reacted with a DEN-2 type-specific neutralizing monoclonal antibody (3H5), DEN-2 hyperimmune mouse ascitic fluid, and DEN-2 immune human sera. When administered to mice, DEN-2(B)/MBP elicited a DEN-2 virus neutralizing antibody response that conferred partial protection against challenge infection with a lethal dose of DEN-2 virus administered by intracranial inoculation. In addition, no replication of DEN-2 virus was detectable in the brains of the immunized mice as compared with control mice that were killed six days after challenge. Sera from immunized mice revealed no cross-neutralizing antibody to any of the other DEN serotypes in the plaque-reduction neutralization test. These findings warrant further studies with the DEN-2(B)/MBP antigen as a potential human vaccine candidate. An effective vaccine could prevent thousands of cases of illness and many deaths each year resulting from DEN virus infections.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, env,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/maltose transport system, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0002-9637
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
655-62
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9598457-ATP-Binding Cassette Transporters,
pubmed-meshheading:9598457-Animals,
pubmed-meshheading:9598457-Carrier Proteins,
pubmed-meshheading:9598457-Dengue,
pubmed-meshheading:9598457-Dengue Virus,
pubmed-meshheading:9598457-Disease Models, Animal,
pubmed-meshheading:9598457-Escherichia coli Proteins,
pubmed-meshheading:9598457-Female,
pubmed-meshheading:9598457-Gene Products, env,
pubmed-meshheading:9598457-Maltose-Binding Proteins,
pubmed-meshheading:9598457-Mice,
pubmed-meshheading:9598457-Mice, Inbred BALB C,
pubmed-meshheading:9598457-Monosaccharide Transport Proteins,
pubmed-meshheading:9598457-Recombinant Fusion Proteins,
pubmed-meshheading:9598457-Survival Analysis
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pubmed:year |
1998
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pubmed:articleTitle |
Evaluation of the protective efficacy of a recombinant dengue envelope B domain fusion protein against dengue 2 virus infection in mice.
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pubmed:affiliation |
Naval Medical Research Institute, Bethesda, Maryland 20889-5607, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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