Evidence map›Paper›PMID 12186887›Full record

ArticleJournal of virology2002

Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize human immunodeficiency virus type 1 primary isolates from various clades.

Miroslaw K Gorny, Constance Williams, Barbara Volsky, Kathy Revesz, Sandra Cohen, Victoria R Polonis, William J Honnen, Samuel C Kayman, Chavdar Krachmarov, Abraham Pinter and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
4.3field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

99 citing papers in PubMed, 177 citations in OpenAlex.

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  20. Structural basis of clade-specific HIV-1 neutralization by humanized anti-V3 monoclonal antibody KD-247.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article

39 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Miroslaw K GornyDepartment of Pathology, New York University School of Medicine, New York, NY 10016, USA.
Constance Williams
Barbara Volsky
Kathy Revesz
Sandra Cohen
Victoria R Polonis
William J Honnen
Samuel C Kayman
Chavdar Krachmarov
Abraham Pinter
Susan Zolla-Pazner
University School · USVeterans Health Administration · US

Funding

VIROLOGY COREP30AI027742 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI GORNY, MIROSLAW K · 1989 to 2010
$19.4M
PROTECTIVE HUMAN MONOCLONAL ANTIBODIES TO HIV1R01HL059725 · NHLBI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ZOLLA-PAZNER, SUSAN B · 1997 to 2014
$8.8M
IMMUNOLOGIC RELATEDNESS AMONG AND BETWEEN HIV-1 SUBTYPESR01AI036085 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ZOLLA-PAZNER, SUSAN B · 1994 to 2008
$5.3M
NHLBI NIH HHS HL59725NHLBI NIH HHS R01 HL059725NIAID NIH HHS AI27742NIAID NIH HHS AI36085NIAID NIH HHS P30 AI027742NIAID NIH HHS R01 AI036085
6 · The paper itself

Abstract

The epitopes of the V3 domain of the human immunodeficiency virus type 1 (HIV-1) gp120 glycoprotein have complex structures consisting of linear and conformational antigenic determinants. Anti-V3 antibodies (Abs) recognize both types of elements, but Abs which preferentially react to the conformational aspect of the epitopes may have more potent neutralizing activity against HIV-1, as recently suggested. To test this hypothesis, human anti-V3 monoclonal Abs (MAbs) were selected using a V3 fusion protein (V3-FP) which retains the conformation of the third variable region. The V3-FP consists of the V3(JR-CSF) sequence inserted into a truncated form of murine leukemia virus gp70. Six human MAbs which recognize epitopes at the crown of the V3 loop were selected with the V3-FP. They were found to react more strongly with molecules displaying conformationally intact V3 than with linear V3 peptides. In a virus capture assay, these MAbs showed cross-clade binding to native, intact virions of clades A, B, C, D, and F. No binding was found to isolates from subtype E. The neutralizing activity of MAbs against primary isolates was determined in three assays: the GHOST cell assay, a phytohemagglutinin-stimulated peripheral blood mononuclear cell assay, and a luciferase assay. While these new MAbs displayed various degrees of activity, the pattern of cross-clade neutralization of clades A, B, and F was most pronounced. The neutralization of clades C and D viruses was weak and sporadic, and neutralization of clade E by these MAbs was not detected. Analysis by linear regression showed a highly significant correlation (P < 0.0001) between the strength of binding of these anti-V3 MAbs to intact virions and the percent neutralization. These studies demonstrate that human MAbs to conformation-sensitive epitopes of V3 display cross-clade reactivity in both binding to native, intact virions and neutralization of primary isolates.

Indexed as

Antibody SpecificityAntibodies, MonoclonalBinding, CompetitiveBinding Sites, AntibodyCell Line, TransformedCross ReactionsEpitopesHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansHybridomasNeutralization TestsPeptide FragmentsProtein ConformationVirionAntibodies, MonoclonalEpitopesHIV AntibodiesHIV Envelope Protein gp120HIV envelope protein gp120 (305-321)Peptide Fragments

Identifiers

PMID12186887
PMCPMC136433
OpenAlexW2145462968

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.