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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0003241,
umls-concept:C0003261,
umls-concept:C0003316,
umls-concept:C0019682,
umls-concept:C0019699,
umls-concept:C0023621,
umls-concept:C0061649,
umls-concept:C0086418,
umls-concept:C0205164,
umls-concept:C0332120,
umls-concept:C0332307,
umls-concept:C1148575,
umls-concept:C1514562,
umls-concept:C1519025,
umls-concept:C1522642,
umls-concept:C1705535
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pubmed:issue |
10
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pubmed:dateCreated |
1996-12-3
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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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0889-2229
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
911-24
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8798976-Amino Acid Sequence,
pubmed-meshheading:8798976-Conserved Sequence,
pubmed-meshheading:8798976-Epitope Mapping,
pubmed-meshheading:8798976-HIV Envelope Protein gp41,
pubmed-meshheading:8798976-HIV-1,
pubmed-meshheading:8798976-Humans,
pubmed-meshheading:8798976-Immunoglobulin Fab Fragments,
pubmed-meshheading:8798976-Molecular Sequence Data,
pubmed-meshheading:8798976-Peptide Library,
pubmed-meshheading:8798976-Recombinant Proteins,
pubmed-meshheading:8798976-Sequence Alignment
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pubmed:year |
1996
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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.
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pubmed:affiliation |
Department of Immunology, Scripps Research Institute, La Jolla, California 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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