Evidence map›Paper›PMID 22826297›Full record

ArticleThe Journal of experimental medicine2012

Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein.

Florian Klein, Christian Gaebler, Hugo Mouquet, D Noah Sather, Clara Lehmann, Johannes F Scheid, Zane Kraft, Yan Liu, John Pietzsch, Arlene Hurley and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed, 1 pooled it
10.7field-weighted citation impact, top 1% 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

113 citing papers in PubMed, 1 synthesis or guideline pooled it, 151 citations in OpenAlex.

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  16. A cell-cell interaction format for selection of high-affinity antibodies to membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019
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53 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

18 authors at 11 institutions in 3 countries.

Florian KleinLaboratory of Molecular Immunology, The Rockefeller University, New York, NY 10065, USA.
Christian Gaebler
Hugo Mouquet
D Noah Sather
Clara Lehmann
Johannes F Scheid
Zane Kraft
Yan Liu
John Pietzsch
Arlene Hurley
Pascal Poignard
Ten Feizi
Lynn Morris
Bruce D Walker
Gerd Fätkenheuer
Michael S Seaman
Leonidas Stamatatos
Michel C Nussenzweig
Center for Infectious Disease Research · USRockefeller University · USHoward Hughes Medical Institute · USImperial College London · GBUniversity Hospital Cologne · DEBeth Israel Deaconess Medical Center · USInternational AIDS Vaccine Initiative · USNational Institute for Communicable DiseasesRagon Institute of MGH, MIT and Harvard · USRockefeller University Hospital · USUniversity Hospital Carl Gustav Carus · DE

Funding

Protein Expression CoreP01AI081677 · NIAID · ROCKEFELLER UNIVERSITY · PI RAVETCH, JEFFREY VICTOR · 2009 to 2013
$10.6M
Immunogenic sugar moieties of prostate cancersU01CA128416 · NCI · STANFORD UNIVERSITY · PI WANG, DENONG · 2007 to 2011
$2.3M
NCI NIH HHS U01 CA128416NCI NIH HHS U01CA128416NIAID NIH HHS 1 PO1 AI081677NIAID NIH HHS P01 AI081677
6 · The paper itself

Abstract

Two to three years after infection, a fraction of HIV-1-infected individuals develop serologic activity that neutralizes most viral isolates. Broadly neutralizing antibodies that recognize the HIV-1 envelope protein have been isolated from these patients by single-cell sorting and by neutralization screens. Here, we report a new method for anti-HIV-1 antibody isolation based on capturing single B cells that recognize the HIV-1 envelope protein expressed on the surface of transfected cells. Although far less efficient than soluble protein baits, the cell-based capture method identified antibodies that bind to a new broadly neutralizing epitope in the vicinity of the V3 loop and the CD4-induced site (CD4i). The new epitope is expressed on the cell surface form of the HIV-1 spike, but not on soluble forms of the same envelope protein. Moreover, the new antibodies complement the neutralization spectrum of potent broadly neutralizing anti-CD4 binding site (CD4bs) antibodies obtained from the same individual. Thus, combinations of potent broadly neutralizing antibodies with complementary activity can account for the breadth and potency of naturally arising anti-HIV-1 serologic activity. Therefore, vaccines aimed at eliciting anti-HIV-1 serologic breadth and potency should not be limited to single epitopes.

Indexed as

Antibodies, NeutralizingBinding Sites, AntibodyB-LymphocytesCD4 AntigensEpitopesHEK293 CellsHIV-1HIV AntibodiesHIV Envelope Protein gp160HIV InfectionsHumansAntibodies, NeutralizingCD4 AntigensEpitopesHIV AntibodiesHIV Envelope Protein gp160

Identifiers

PMID22826297
PMCPMC3409500
OpenAlexW2072974935

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.