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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1992-10-13
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pubmed:abstractText |
Different parts of the human immunodeficiency virus type 1 and type 2 (HIV-1 and HIV-2) integrase proteins were expressed as TrpE fusion proteins in Escherichia coli and used to screen human sera. In the immunoblot, all HIV/integrase-positive human sera tested reacted with the carboxy-terminal third of the integrase protein. Furthermore, they crossreacted with the same part of the heterologous protein. Half (50%) of the HIV-1/integrase-positive sera additionally detected antigenic epitopes in the amino-terminal third of the HIV-1 protein. Two of the recombinant proteins were used to generate polyclonal rabbit sera, which react with type-common epitopes of both integrase proteins. To map the B-cell epitopes of the HIV integrase proteins in more detail, overlapping decapeptides representing the entire integrase proteins of HIV-1 and HIV-2 were synthesized and used in a pin-based oligopeptide ELISA to scan human sera. This method can define three potential immunogenic epitopes of the HIV-1 integrase and one potential epitope of the HIV-2 integrase. The immunodominant epitopes of the HIV-1 integrase, one localized in the amino-terminal (IDKAQDEHEKYHSNWRAM), one in the central (QMAVFIHNFKRKGGIGGY), and one in the carboxy-terminal (AVVIQDNSDIKVVPRRK) part of the protein were synthesized as oligopeptides and used to test a larger panel of human sera in ELISA (156 HIV-1+ sera and 104 HIV-1- sera). The amino- and the carboxy-terminal epitopes were of equivalent reactivity, while the central part of the HIV-1 integrase seems to be less immunogenic. Nearly 90% of the HIV-1/integrase-positive human sera could be detected by a combination of these three peptides.
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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/DNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Immunodominant Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Integrases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0889-2229
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1301-10
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1520543-Amino Acid Sequence,
pubmed-meshheading:1520543-Animals,
pubmed-meshheading:1520543-DNA Nucleotidyltransferases,
pubmed-meshheading:1520543-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:1520543-Escherichia coli,
pubmed-meshheading:1520543-HIV Seropositivity,
pubmed-meshheading:1520543-HIV-1,
pubmed-meshheading:1520543-HIV-2,
pubmed-meshheading:1520543-Humans,
pubmed-meshheading:1520543-Immunoblotting,
pubmed-meshheading:1520543-Immunodominant Epitopes,
pubmed-meshheading:1520543-Integrases,
pubmed-meshheading:1520543-Molecular Sequence Data,
pubmed-meshheading:1520543-Peptides,
pubmed-meshheading:1520543-Recombinant Proteins
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pubmed:year |
1992
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pubmed:articleTitle |
Mapping of immunodominant epitopes of the HIV-1 and HIV-2 integrase proteins by recombinant proteins and synthetic peptides.
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pubmed:affiliation |
Abteilung Virologie, Universitätsklinikum, Homburg/Saar, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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