| pubmed-article:11124838 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11124838 | lifeskim:mentions | umls-concept:C0019169 | lld:lifeskim |
| pubmed-article:11124838 | lifeskim:mentions | umls-concept:C0086097 | lld:lifeskim |
| pubmed-article:11124838 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:11124838 | lifeskim:mentions | umls-concept:C0032105 | lld:lifeskim |
| pubmed-article:11124838 | lifeskim:mentions | umls-concept:C0053358 | lld:lifeskim |
| pubmed-article:11124838 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:11124838 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:11124838 | pubmed:dateCreated | 2001-1-8 | lld:pubmed |
| pubmed-article:11124838 | 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. | lld:pubmed |
| pubmed-article:11124838 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11124838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11124838 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11124838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11124838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11124838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11124838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11124838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11124838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11124838 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11124838 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11124838 | pubmed:issn | 0270-9139 | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:MartinMM | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:RuchetonMM | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:CeruttiMM | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:SeigneurinJ... | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:StefanRR | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:GraaflandHH | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:ZarskiJ PJP | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:VeasFF | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:D'AngeacA DAD | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:BossyJ PJP | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:Morel-Baccard... | lld:pubmed |
| pubmed-article:11124838 | pubmed:author | pubmed-author:MisséDD | lld:pubmed |
| pubmed-article:11124838 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11124838 | pubmed:volume | 33 | lld:pubmed |
| pubmed-article:11124838 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11124838 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11124838 | pubmed:pagination | 207-17 | lld:pubmed |
| pubmed-article:11124838 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11124838 | pubmed:meshHeading | pubmed-meshheading:11124838... | lld:pubmed |
| pubmed-article:11124838 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11124838 | pubmed:articleTitle | Hepatitis B virus Dane particles bind to human plasma apolipoprotein H. | lld:pubmed |
| pubmed-article:11124838 | pubmed:affiliation | Laboratoire d'Immunologie Rétrovirale et Moléculaire IRD UR34, Centre Régional de Transfusion Sanguine, Montpellier, France. stefas@melusine.mpl.orstrom.fr | lld:pubmed |
| pubmed-article:11124838 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11124838 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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