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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2004-4-28
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pubmed:abstractText |
One strategy for the generation of broadly reactive neutralizing antibodies (NA) against human immunodeficiency virus type 1 (HIV-1) primary isolates is to use immunogens that have constrained HIV-1 envelope gp120 conformations reflective of triggered envelope on the surface of virions. A major change in gp120 following binding to CD4 is the enhanced exposure of the CCR5 binding site. One inducer of CCR5 binding site epitopes on gp120 is the human anti-gp120 monoclonal antibody, A32. We have made cross-linked A32-rgp120(89.6) and A32-rgp120(BaL) complexes and have compared their immunogenicities to those of uncomplexed recombinant gp120(BaL) (rgp120(BaL)) and rgp120(89.6). A32-rgp120(89.6) and A32-rgp120(BaL) complexes had stable induced CCR5 binding site expression compared to that of uncomplexed rgp120s. However, the A32-rgp120 complexes had similar capacities in guinea pigs for induction of NA against HIV-1 primary isolates versus that of rgp120 alone. A32-rgp120(89.6) induced antibodies that neutralized 6 out of 11 HIV-1 isolates, while rgp120(89.6) alone induced antibodies that neutralized 4 out of 11 HIV-1 isolates. A32-rgp120(BaL) complexes induced antibodies that neutralized 4 out of 14 HIV-1 isolates while, surprisingly, non-cross-linked rgp120(BaL) induced antibodies that neutralized 9 out of 14 (64%) HIV-1 isolates. Thus, stable enhanced expression of the coreceptor binding site on constrained gp120 is not sufficient for inducing broadly neutralizing anti-HIV-1 NA. Moreover, the ability of HIV-1 rgp120(BaL) to induce antibodies that neutralized approximately 60% of subtype B HIV-1 isolates warrants consideration of using HIV-1 BaL as a starting point for immunogen design for subtype B HIV-1 experimental immunogens.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-10358771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-11090138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-11160726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-11287566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-11602749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-11782464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-11967298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-12089434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-12192089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-12584309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-12829768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-14581570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-7543586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-7544051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-8568294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-8615032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-9151820,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-9421642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-9499039,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-9499040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-9499111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15113908-9733838
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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 |
May
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5270-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2004
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pubmed:articleTitle |
Immunogenicity of constrained monoclonal antibody A32-human immunodeficiency virus (HIV) Env gp120 complexes compared to that of recombinant HIV type 1 gp120 envelope glycoproteins.
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pubmed:affiliation |
Duke Human Vaccine Institute and Department of Medicine, Duke University School of Medicine, Durham, NC 27710, USA. liao0001@mc.duke.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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