Evidence map›Paper›PMID 28630473›Full record

ArticleScientific reports2017

Impact of Antigen Density on the Binding Mechanism of IgG Antibodies.

Maya Hadzhieva, Anastas D Pashov, Srinivas Kaveri, Sébastien Lacroix-Desmazes, Hugo Mouquet, Jordan D Dimitrov

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

30 citing papers in PubMed, 49 citations in OpenAlex.

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  3. Multivalency Enables Signal Processing at Single Protein Level.Journal of the American Chemical Society · 2025
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  8. Serum immunoglobulin and the threshold of Fc receptor-mediated immune activation.Biochimica et biophysica acta. General subjects · 2023
    Review
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  13. Review
  14. Article
  15. Mucosal Delivery of HIV-1 Glycoprotein Vaccine Candidate Enabled by Short Carbon Nanotubes.Particle & particle systems characterization : measurement and description of particle properties and behavior in powders and other disperse systems · 2022
    Article
  16. Review
  17. Review
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  20. Article
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

6 authors at 4 institutions in 2 countries.

Maya HadzhievaInstitute of Microbiology, Bulgarian Academy of Sciences, 1113, Sofia, Bulgaria.
Anastas D PashovInstitute of Microbiology, Bulgarian Academy of Sciences, 1113, Sofia, Bulgaria.
Srinivas KaveriSorbonne Universités, UPMC Univ Paris 06, UMR_S 1138, Centre de Recherche des Cordeliers, 75006, Paris, France.
Sébastien Lacroix-DesmazesSorbonne Universités, UPMC Univ Paris 06, UMR_S 1138, Centre de Recherche des Cordeliers, 75006, Paris, France.
Hugo MouquetLaboratory of Humoral Response to Pathogens, Department of Immunology, Institut Pasteur, and INSERM U1222, 75015, Paris, France.
Jordan D DimitrovSorbonne Universités, UPMC Univ Paris 06, UMR_S 1138, Centre de Recherche des Cordeliers, 75006, Paris, France. jordan.dimitrov@crc.jussieu.fr.
Centre de Recherche des Cordeliers · FRSorbonne Université · FRDélégation Paris 5 · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The density and distribution pattern of epitopes at the surface of pathogens have a profound impact on immune responses. Although multiple lines of evidence highlight the significance of antigen surface density for antibody binding, a quantitative description of its effect on recognition mechanisms is missing. Here, we analyzed binding kinetics and thermodynamics of six HIV-1 neutralizing antibodies as a function of the surface density of envelope glycoprotein gp120. Antibodies that recognize gp120 with low to moderate binding affinity displayed the most pronounced sensitivity to variation in antigen density, with qualitative and substantial quantitative changes in the energetics of the binding process as revealed by non-equilibrium and equilibrium thermodynamic analyses. In contrast, the recognition of gp120 by the antibodies with the highest affinity was considerably less influenced by variations in antigen density. These data suggest that a lower affinity of antibodies permits higher dynamics during the antigen recognition process, which may have considerable functional repercussions. These findings contribute to a better understanding of the mechanisms of antigen recognition by antibodies. They are also of importance for apprehending the impact of antigen topology on immune-defense functions of antibodies.

Indexed as

Antibody AffinityAntibodies, NeutralizingAntigens, ViralHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansImmunoglobulin GAntibodies, NeutralizingAntigens, Viralgp120 protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp120Immunoglobulin G

Identifiers

PMID28630473
PMCPMC5476644
OpenAlexW2626346231

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.