Evidence map›Paper›PMID 21543485›Full record

ArticleJournal of virology2011

An HIV-1 gp120 envelope human monoclonal antibody that recognizes a C1 conformational epitope mediates potent antibody-dependent cellular cytotoxicity (ADCC) activity and defines a common ADCC epitope in human HIV-1 serum.

Guido Ferrari, Justin Pollara, Daniel Kozink, Tiara Harms, Mark Drinker, Stephanie Freel, M Anthony Moody, S Munir Alam, Georgia D Tomaras, Christina Ochsenbauer and 5 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 180 papers.

0numbers the graph read from it
0cells of the map it votes in
180citing papers in PubMed
6.2field-weighted citation impact, top 2% 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

180 citing papers in PubMed, 239 citations in OpenAlex.

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  14. Activation of CXCR3Journal of virology · 2025
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120 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

15 authors at 4 institutions in 1 country.

Guido FerrariDuke University Medical Center, Department of Surgery, P.O. Box 2926, Durham, NC 27710, USA. gflmp@duke.edu
Justin Pollara
Daniel Kozink
Tiara Harms
Mark Drinker
Stephanie Freel
M Anthony Moody
S Munir Alam
Georgia D Tomaras
Christina Ochsenbauer
John C Kappes
George M Shaw
James A Hoxie
James E Robinson
Barton F Haynes
Duke University · USUniversity of Alabama at Birmingham · USTulane University · USUniversity of Pennsylvania · US

Funding

Virology CoreP30AI027767 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Paul A. Goepfert · 1988 to 2026
$84.1M
Social and Behavioral Sciences CoreP30AI064518 · NIAID · DUKE UNIVERSITY · PI Susanna Naggie, GEORGIA Doris TOMARAS · 2005 to 2026
$50.5M
Ruth L. Kirschstein National Research Service Award (NRSA)- T32T32AI007392 · NIAID · DUKE UNIVERSITY · PI Amy Lynn Corneli, Guido Ferrari · 1990 to 2026
$9.8M
Poly-functional analyses of vaccine-induced T cell responsesR01AI050483 · NIAID · DUKE UNIVERSITY · PI FERRARI, GUIDO · 2001 to 2010
$3.5M
NIAID NIH HHS 5R01AI050483-09NIAID NIH HHS AI07392NIAID NIH HHS P30 AI027767NIAID NIH HHS P30 AI064518NIAID NIH HHS P30-AI-27767NIAID NIH HHS P30-AI-64518NIAID NIH HHS R01 AI050483NIAID NIH HHS T32 AI007392PHS HHS A1067854-03
6 · The paper itself

Abstract

Among nonneutralizing HIV-1 envelope antibodies (Abs), those capable of mediating antibody-dependent cellular cytotoxicity (ADCC) activity have been postulated to be important for control of HIV-1 infection. ADCC-mediating Ab must recognize HIV-1 antigens expressed on the membrane of infected cells and bind the Fcγ receptor (FcR) of the effector cell population. However, the precise targets of serum ADCC antibody are poorly characterized. The human monoclonal antibody (MAb) A32 is a nonneutralizing antibody isolated from an HIV-1 chronically infected person. We investigated the ability of MAb A32 to recognize HIV-1 envelope expressed on the surface of CD4(+) T cells infected with primary and laboratory-adapted strains of HIV-1, as well as its ability to mediate ADCC activity. The MAb A32 epitope was expressed on the surface of HIV-1-infected CD4(+) T cells earlier than the CD4-inducible (CD4i) epitope bound by MAb 17b and the gp120 carbohydrate epitope bound by MAb 2G12. Importantly, MAb A32 was a potent mediator of ADCC activity. Finally, an A32 Fab fragment blocked the majority of ADCC-mediating Ab activity in plasma of subjects chronically infected with HIV-1. These data demonstrate that the epitope defined by MAb A32 is a major target on gp120 for plasma ADCC activity.

Indexed as

Antibodies, MonoclonalAntibody-Dependent Cell CytotoxicityCD4-Positive T-LymphocytesCell LineEpitopesFluorescent Antibody Technique, IndirectHIV-1HIV Envelope Protein gp120HIV InfectionsHumansProtein ConformationAntibodies, MonoclonalEpitopesHIV Envelope Protein gp120

Identifiers

PMID21543485
PMCPMC3126567
OpenAlexW2019405644

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.