pubmed-article:18480440 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C0206679 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C0282682 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C1654934 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C1423085 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C0444454 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:18480440 | lifeskim:mentions | umls-concept:C0061666 | lld:lifeskim |
pubmed-article:18480440 | pubmed:issue | 14 | lld:pubmed |
pubmed-article:18480440 | pubmed:dateCreated | 2008-6-27 | lld:pubmed |
pubmed-article:18480440 | pubmed:abstractText | Herpes simplex virus type 1 (HSV-1) glycoprotein C (gC) blocks complement activation, and glycoprotein E (gE) interferes with IgG Fc-mediated activities. While evaluating gC- and gE-mediated immune evasion in human immunodeficiency virus (HIV)-HSV-1-coinfected subjects, we noted that antibody alone was more effective at neutralizing a strain with mutations in gC and gE (gC/gE) than a wild-type (WT) virus. This result was unexpected since gC and gE are postulated to interfere with complement-mediated neutralization. We used pooled human immunoglobulin G (IgG) from HIV-negative donors to confirm the results and evaluated mechanisms of the enhanced antibody neutralization. We demonstrated that differences in antibody neutralization cannot be attributed to the concentrations of HSV-1 glycoproteins on the two viruses or to the absence of an IgG Fc receptor on the gC/gE mutant virus or to enhanced neutralization of the mutant virus by antibodies that target only gB, gD, or gH/gL, which are the glycoproteins involved in virus entry. Since sera from HIV-infected subjects and pooled human IgG contain antibodies against multiple glycoproteins, we determined whether differences in neutralization become apparent when antibodies to gB, gD, or gH/gL are used in combination. Neutralization of the gC/gE mutant was greatly increased compared that of WT virus when any two of the antibodies against gB, gD, or gH/gL were used in combination. These results suggest that gC and gE on WT virus provide a shield against neutralizing antibodies that interfere with gB-gD, gB-gH/gL, or gD-gH/gL interactions and that one function of virus neutralization is to prevent interactions between these glycoproteins. | lld:pubmed |
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pubmed-article:18480440 | pubmed:language | eng | lld:pubmed |
pubmed-article:18480440 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18480440 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18480440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18480440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18480440 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18480440 | pubmed:month | Jul | lld:pubmed |
pubmed-article:18480440 | pubmed:issn | 1098-5514 | lld:pubmed |
pubmed-article:18480440 | pubmed:author | pubmed-author:MingJiangJ | lld:pubmed |
pubmed-article:18480440 | pubmed:author | pubmed-author:FriedmanHarve... | lld:pubmed |
pubmed-article:18480440 | pubmed:author | pubmed-author:HookLauren... | lld:pubmed |
pubmed-article:18480440 | pubmed:author | pubmed-author:HodinkaRichar... | lld:pubmed |
pubmed-article:18480440 | pubmed:author | pubmed-author:HuangJialingJ | lld:pubmed |
pubmed-article:18480440 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18480440 | pubmed:volume | 82 | lld:pubmed |
pubmed-article:18480440 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18480440 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18480440 | pubmed:pagination | 6935-41 | lld:pubmed |
pubmed-article:18480440 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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