Evidence map›Paper›PMID 22219363›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Enhanced HIV-1 neutralization by antibody heteroligation.

Hugo Mouquet, Malte Warncke, Johannes F Scheid, Michael S Seaman, Michel C Nussenzweig

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 55 citations in OpenAlex.

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  6. B cell signaling in context.Nature immunology · 2019
    Review
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  8. Article
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  14. Bispecific antibodies for viral immunotherapy.Human vaccines & immunotherapeutics · 2017
    Review
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  17. Article
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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

5 authors at 4 institutions in 3 countries.

Hugo MouquetLaboratory of Molecular Immunology, The Rockefeller University, New York, NY 10065, USA. hmouquet@rockefeller.edu
Malte Warncke
Johannes F Scheid
Michael S Seaman
Michel C Nussenzweig
Center of Molecular Immunology (Cuba) · CUBeth Israel Deaconess Medical Center · USRockefeller University · USUniversität Hamburg · DE

Funding

Protein Expression CoreP01AI081677 · NIAID · ROCKEFELLER UNIVERSITY · PI STEINMAN, RALPH MARVIN · 2009 to 2013
$10.6M
Howard Hughes Medical InstituteNIAID NIH HHS P01 AI081677
6 · The paper itself

Abstract

Passive transfer of broadly neutralizing human antibodies against HIV-1 protects macaques against infection. However, HIV-1 uses several strategies to escape antibody neutralization, including mutation of the gp160 viral surface spike, a glycan shield to block antibody access to the spike, and expression of a limited number of viral surface spikes, which interferes with bivalent antibody binding. The latter is thought to decrease antibody apparent affinity or avidity, thereby interfering with neutralizing activity. To test the idea that increasing apparent affinity might enhance neutralizing activity, we engineered bispecific anti-HIV-1 antibodies (BiAbs) that can bind bivalently by virtue of one scFv arm that binds to gp120 and a second arm to the gp41 subunit of gp160. The individual arms of the BiAbs preserved the binding specificities of the original anti-HIV IgG antibodies and together bound simultaneously to gp120 and gp41. Heterotypic bivalent binding enhanced neutralization compared with the parental antibodies. We conclude that antibody recognition and viral neutralization of HIV can be improved by heteroligation.

Indexed as

Antibodies, BispecificAntibodies, NeutralizingAntigens, ViralHEK293 CellsHIV-1HIV AntibodiesHIV Envelope Protein gp120HIV Envelope Protein gp41HumansImmunoglobulin GNeutralization TestsProtein BindingProtein EngineeringSingle-Chain AntibodiesAntibodies, BispecificAntibodies, NeutralizingAntigens, ViralHIV AntibodiesHIV Envelope Protein gp120HIV Envelope Protein gp41Immunoglobulin GSingle-Chain Antibodies

Identifiers

PMID22219363
PMCPMC3271928
OpenAlexW2015631175

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.