Evidence map›Paper›PMID 28122982›Full record

ArticleJournal of virology2017

Lack of ADCC Breadth of Human Nonneutralizing Anti-HIV-1 Antibodies.

Timothée Bruel, Florence Guivel-Benhassine, Valérie Lorin, Hugues Lortat-Jacob, Françoise Baleux, Katia Bourdic, Nicolas Noël, Olivier Lambotte, Hugo Mouquet, Olivier Schwartz

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

57 citing papers in PubMed, 72 citations in OpenAlex.

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  16. Engaging innate immunity in HIV-1 cure strategies.Nature reviews. Immunology · 2022
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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

10 authors at 8 institutions in 1 country.

Timothée BruelVirus and Immunity Unit, Department of Virology, Institut Pasteur, Paris, France.
Florence Guivel-BenhassineVirus and Immunity Unit, Department of Virology, Institut Pasteur, Paris, France.
Valérie LorinLaboratory of Humoral Response to Pathogens, Department of Immunology, Institut Pasteur, Paris, France.
Hugues Lortat-JacobInstitut de Biologie Structurale, UMR5075 CNRS, CEA, Université Grenoble-Alpes, Grenoble, France.
Françoise BaleuxInstitut Pasteur, Unité de Chimie des Biomolécules, UMR CNRS 3523, Paris, France.
Katia BourdicUniversité Paris Sud, UMR-1184, Paris, France.
Nicolas NoëlUniversité Paris Sud, UMR-1184, Paris, France.
Olivier LambotteUniversité Paris Sud, UMR-1184, Paris, France.
Hugo MouquetLaboratory of Humoral Response to Pathogens, Department of Immunology, Institut Pasteur, Paris, France hugo.mouquet@pasteur.fr schwartz@pasteur.fr.
Olivier SchwartzVirus and Immunity Unit, Department of Virology, Institut Pasteur, Paris, France hugo.mouquet@pasteur.fr schwartz@pasteur.fr.
Institut Pasteur · FRUniversité Paris-Sud · FRCentre National de la Recherche Scientifique · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRDepartment of Virology · FRHôpitaux Universitaires Paris-Ouest · FRInserm · FRInstitut de Recherche Vaccinale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Anti-human immunodeficiency virus type 1 (HIV-1) nonneutralizing antibodies (nnAbs) capable of antibody-dependent cellular cytotoxicity (ADCC) have been identified as a protective immune correlate in the RV144 vaccine efficacy trial. Broadly neutralizing antibodies (bNAbs) also mediate ADCC in cell culture and rely on their Fc region for optimal efficacy in animal models. Here, we selected 9 monoclonal nnAbs and 5 potent bNAbs targeting various epitopes and conformations of the gp120/41 complex and analyzed the potency of the two types of antibodies to bind and eliminate HIV-1-infected cells in culture. Regardless of their neutralizing activity, most of the selected antibodies recognized and killed cells infected with two laboratory-adapted HIV-1 strains. Some nnAbs also bound bystander cells that may have captured viral proteins. However, in contrast to the bNAbs, the nnAbs bound poorly to reactivated infected cells from 8 HIV-positive individuals and did not mediate effective ADCC against these cells. The nnAbs also inefficiently recognize cells infected with 8 different transmitted-founder (T/F) isolates. The addition of a synthetic CD4 mimetic enhanced the binding and killing efficacy of some of the nnAbs in an epitope-dependent manner without reaching the levels achieved by the most potent bNAbs. Overall, our data reveal important qualitative and quantitative differences between nnAbs and bNAbs in their ADCC capacity and strongly suggest that the breadth of recognition of HIV-1 by nnAbs is narrow.

Indexed as

Antibody-Dependent Cell CytotoxicityAntibodies, MonoclonalCells, CulturedHIV-1HIV AntibodiesHIV Envelope Protein gp120HIV Envelope Protein gp41HumansAntibodies, Monoclonalgp120 protein, Human immunodeficiency virus 1gp41 protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp120HIV Envelope Protein gp41ADCCHIV-1monoclonal antibodiesneutralizing antibodiesnonneutralizing antibodiesreservoir

Identifiers

PMID28122982
PMCPMC5375671
OpenAlexW2582676572

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.