Source:http://linkedlifedata.com/resource/pubmed/id/11162801
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2001-2-22
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| pubmed:abstractText |
Three of 41 IgM monoclonal antibodies derived from dengue 1 virus immunized mice neutralized dengue 1 infection in vitro. All three neutralizing monoclonal antibodies reacted with spatially related epitopes on the E protein of dengue 1 which were also recognized by antibodies in sera from dengue patients. Two neutralization-resistant populations of dengue 1 virus, D1-M10 and D1-M17, were selected by sequential passage of virus in C6/36 cells in the presence of neutralizing IgM monoclonal antibodies M10 and M17, respectively. Single nucleotide changes occurred in the E protein gene of each of these virus populations resulting in single amino acid substitutions at E279 (Phe-Ser) in D1-M10 and at E293 (Thr-Ile) in D1-M17. Both neutralization-resistant populations of virus were more sensitive to elevated temperature than was the wild-type dengue 1 virus and the infectivity and haemagglutinating ability of the neutralization-resistant populations decreased more slowly than that of wild-type virus when exposed to pH in the range 5.8 to 7.0. These are the first epitopes involved in neutralization to have been identified in dengue 1 virus and the first outside domain III of the E protein on any dengue virus.
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| pubmed:language |
eng
|
| 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/Antibodies, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/E protein TH Sman, Dengue virus,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Hemagglutinins, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Immune Sera,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
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| pubmed:issn |
0042-6822
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
20
|
| pubmed:volume |
279
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
447-58
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| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:11162801-Amino Acid Substitution,
pubmed-meshheading:11162801-Animals,
pubmed-meshheading:11162801-Antibodies, Monoclonal,
pubmed-meshheading:11162801-Antibodies, Viral,
pubmed-meshheading:11162801-Cell Line,
pubmed-meshheading:11162801-Dengue Virus,
pubmed-meshheading:11162801-Epitopes,
pubmed-meshheading:11162801-Hemagglutinins, Viral,
pubmed-meshheading:11162801-Humans,
pubmed-meshheading:11162801-Hydrogen-Ion Concentration,
pubmed-meshheading:11162801-Immune Sera,
pubmed-meshheading:11162801-Immunoglobulin M,
pubmed-meshheading:11162801-Mice,
pubmed-meshheading:11162801-Models, Structural,
pubmed-meshheading:11162801-Mutation,
pubmed-meshheading:11162801-Neutralization Tests,
pubmed-meshheading:11162801-Temperature,
pubmed-meshheading:11162801-Viral Envelope Proteins
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| pubmed:year |
2001
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| pubmed:articleTitle |
Epitopes on the dengue 1 virus envelope protein recognized by neutralizing IgM monoclonal antibodies.
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| pubmed:affiliation |
Centre for Molecular Biotechnology, School of Life Sciences, Queensland University of Technology, 2 George Street, Brisbane, Queensland, 4000, Australia.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|