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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2001-1-8
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pubmed:abstractText |
Human apolipoprotein H (apo H) was found to bind specifically to hepatitis B surface antigen (HBsAg) from hepatitis B virus (HBV)-infected individuals. We used recombinant HBsAg proteins to analyze HBV domains recognized by apo H. We showed that the myristylated pre-S1 domain of HBsAg strongly interacted with apo H. This binding involved phospholipid components of the HBV envelope because their removal by detergent prevented apo H-HBsAg interaction. The opposite effects of iron and zinc metal ions on binding suggest that the oxidation of phospholipids also affects apo H-HBsAg interaction. After fractionation of viral particles on a sucrose gradient, and their addition to microtiter plates coated with apo H or anti-HBsAg, we observed that the maximal anti-HBsAg capture activity corresponded to a sucrose concentration of 36%, whereas the maximal apo H capture activity corresponded to a concentration of 39%. Electron microscopy and polymerase chain reaction (PCR) Southern blot studies of these fractions showed that the fraction with maximal apo H binding predominantly contained full Dane particles. Finally, we studied apo H-HBsAg binding relative to the presence of hepatitis B virus markers and observed that apo H binding activity for HBsAg was higher in sera from patients in the active virus replication phase.
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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 |
Jan
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pubmed:issn |
0270-9139
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pubmed:author |
pubmed-author:BossyJ PJP,
pubmed-author:CeruttiMM,
pubmed-author:D'AngeacA DAD,
pubmed-author:GraaflandHH,
pubmed-author:MartinMM,
pubmed-author:MisséDD,
pubmed-author:Morel-BaccardCC,
pubmed-author:RuchetonMM,
pubmed-author:SeigneurinJ MJM,
pubmed-author:StefanRR,
pubmed-author:VeasFF,
pubmed-author:ZarskiJ PJP
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pubmed:issnType |
Print
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
207-17
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11124838-Animals,
pubmed-meshheading:11124838-Blotting, Southern,
pubmed-meshheading:11124838-Cell Line,
pubmed-meshheading:11124838-DNA, Viral,
pubmed-meshheading:11124838-Glycoproteins,
pubmed-meshheading:11124838-Hepatitis B Surface Antigens,
pubmed-meshheading:11124838-Hepatitis B virus,
pubmed-meshheading:11124838-Humans,
pubmed-meshheading:11124838-Immunoenzyme Techniques,
pubmed-meshheading:11124838-Macromolecular Substances,
pubmed-meshheading:11124838-Microscopy, Electron,
pubmed-meshheading:11124838-Oxidation-Reduction,
pubmed-meshheading:11124838-Phospholipids,
pubmed-meshheading:11124838-Polymerase Chain Reaction,
pubmed-meshheading:11124838-Recombinant Proteins,
pubmed-meshheading:11124838-Spodoptera,
pubmed-meshheading:11124838-beta 2-Glycoprotein I
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pubmed:year |
2001
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pubmed:articleTitle |
Hepatitis B virus Dane particles bind to human plasma apolipoprotein H.
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pubmed:affiliation |
Laboratoire d'Immunologie Rétrovirale et Moléculaire IRD UR34, Centre Régional de Transfusion Sanguine, Montpellier, France. stefas@melusine.mpl.orstrom.fr
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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