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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1993-4-13
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pubmed:abstractText |
The possible contribution of Ag-specific Ig receptors on B cells to syncytium formation with HIV-1 envelope (env)-expressing cells was examined. A unique model system was designed that used anti-TNP/TNP interactions between a panel of TNP-specific human B cell lines and TNP-haptenated HIV-1 env-expressing T cells. The prototype B cell line 1:13 (CD4dull) produced few syncytia with vaccinia gp120/41-infected CD4- T cell effectors. However, TNP-haptenation of the HIV-1 env-expressing cells resulted in a five- to 10-fold increase in syncytium formation. The "enhanced" syncytia were blocked by OKT4A mAb, soluble CD4, anti-TNP serum, and TNP-BSA, suggesting a role for both CD4 and Ig receptors. In contrast, the number of syncytia formed between CD4+ CEM T cells and TNP-haptenated effectors was reduced by 30 to 40%, compared with the unhaptenated effectors, suggesting that a fraction of the TNP haptens bound close to the CD4 binding regions on the gp120 envelope, which was confirmed by other experiments. The possibility that B cells specific for the CD4 binding site on HIV-1 gp120 may be involved in syncytium formation with HIV-1 env-expressing cells was tested by screening a panel of five hybrid B cell lines from HIV-1-seropositive individuals. One of these lines produced anti-gp120 antibodies, which bound near the CD4 binding site, and also formed syncytia with HIV-1 env-expressing cells. This study suggests that, in addition to CD4 receptors, certain B cell Ig receptors that bind to gp120 may induce conformational changes leading to cell fusion and their elimination.
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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/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, B-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc,
http://linkedlifedata.com/resource/pubmed/chemical/Trinitrobenzenes
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
150
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2506-16
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7680694-Antigens, CD4,
pubmed-meshheading:7680694-B-Lymphocytes,
pubmed-meshheading:7680694-Cell Fusion,
pubmed-meshheading:7680694-Cell Line,
pubmed-meshheading:7680694-Cell Line, Transformed,
pubmed-meshheading:7680694-Epitopes,
pubmed-meshheading:7680694-HIV Envelope Protein gp120,
pubmed-meshheading:7680694-HIV Seropositivity,
pubmed-meshheading:7680694-Herpesvirus 4, Human,
pubmed-meshheading:7680694-Humans,
pubmed-meshheading:7680694-Lymphocyte Depletion,
pubmed-meshheading:7680694-Phenotype,
pubmed-meshheading:7680694-Protein Binding,
pubmed-meshheading:7680694-Receptors, Antigen, B-Cell,
pubmed-meshheading:7680694-Receptors, Fc,
pubmed-meshheading:7680694-T-Lymphocytes,
pubmed-meshheading:7680694-Trinitrobenzenes
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pubmed:year |
1993
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pubmed:articleTitle |
Fusion of human B cell lines with HIV-1 envelope-expressing T cells is enhanced by antigen-specific Ig receptors. Possible mechanism for elimination of gp120-specific B cells in vivo.
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pubmed:affiliation |
Division of Virology, Food and Drug Administration, Bethesda, MD 20892.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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