pubmed-article:8798976 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C1519025 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0019682 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0019699 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0023621 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C1522642 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0003261 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C1148575 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C1705535 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
pubmed-article:8798976 | lifeskim:mentions | umls-concept:C0061649 | lld:lifeskim |
pubmed-article:8798976 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:8798976 | pubmed:dateCreated | 1996-12-3 | lld:pubmed |
pubmed-article:8798976 | pubmed:abstractText | A large panel of human Fab fragments against the gp41 subunit of the HIV-1 envelope glycoprotein was isolated by panning six phage-displayed antibody libraries against recombinant gp41. The libraries were prepared from HIV-1-seropositive donors. Twenty-three Fabs recognizing conformation-dependent determinants on gp41 were isolated. Further selection of libraries against (1) gp41 ligated with Fabs from the initial selection and against (2) a recombinant gp41-containing gp140 protein yielded five additional Fabs. Competition of members of the Fab panel with one another and with previously described antibodies revealed a series of overlapping specificities that were conveniently grouped into three major epitope clusters. The majority of Fabs recognized epitopes involving residues 649-668 (previously known as the cluster II region), numbered using the Los Alamos LAI sequence. A second set of Fabs reacted with an epitope involving residues 584-609 (known as the cluster I region). Another set of Fabs appeared to recognize a third conformational epitope that has been termed the cluster III region. This third Fab epitope group demonstrated some overlap with both clusters I and II in binding assays. None of the Fabs neutralized HIV-1 laboratory strains at biologically significant concentrations. This tends to support the opinion that a vaccine based on the gp41 molecule has the drawback that neutralizing epitopes of gp41 are rare and/or unfavorably presented to the immune system. Analysis of heavy chain sequences revealed common CDR3 motif sequences in several antibodies, which appears to be an interesting consequence of a persistent immune response to conserved antigen structures. | lld:pubmed |
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pubmed-article:8798976 | pubmed:language | eng | lld:pubmed |
pubmed-article:8798976 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8798976 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8798976 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8798976 | pubmed:month | Jul | lld:pubmed |
pubmed-article:8798976 | pubmed:issn | 0889-2229 | lld:pubmed |
pubmed-article:8798976 | pubmed:author | pubmed-author:BurtonD RDR | lld:pubmed |
pubmed-article:8798976 | pubmed:author | pubmed-author:SullivanNN | lld:pubmed |
pubmed-article:8798976 | pubmed:author | pubmed-author:SodroskiJJ | lld:pubmed |
pubmed-article:8798976 | pubmed:author | pubmed-author:BarbasC... | lld:pubmed |
pubmed-article:8798976 | pubmed:author | pubmed-author:PatteeLL | lld:pubmed |
pubmed-article:8798976 | pubmed:author | pubmed-author:DitzelH JHJ | lld:pubmed |
pubmed-article:8798976 | pubmed:author | pubmed-author:BinleyJ MJM | lld:pubmed |
pubmed-article:8798976 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8798976 | pubmed:day | 1 | lld:pubmed |
pubmed-article:8798976 | pubmed:volume | 12 | lld:pubmed |
pubmed-article:8798976 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8798976 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8798976 | pubmed:pagination | 911-24 | lld:pubmed |
pubmed-article:8798976 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:8798976 | pubmed:meshHeading | pubmed-meshheading:8798976-... | lld:pubmed |
pubmed-article:8798976 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8798976 | pubmed:articleTitle | Human antibody responses to HIV type 1 glycoprotein 41 cloned in phage display libraries suggest three major epitopes are recognized and give evidence for conserved antibody motifs in antigen binding. | lld:pubmed |
pubmed-article:8798976 | pubmed:affiliation | Department of Immunology, Scripps Research Institute, La Jolla, California 92037, USA. | lld:pubmed |
pubmed-article:8798976 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8798976 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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