Evidence map›Paper›PMID 29593217›Full record

ArticleNature communications2018

Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope.

Christopher O Barnes, Harry B Gristick, Natalia T Freund, Amelia Escolano, Artem Y Lyubimov, Harald Hartweger, Anthony P West, Aina E Cohen, Michel C Nussenzweig, Pamela J Bjorkman

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
–field-weighted citation impact
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

71 citing papers in PubMed.

  1. Article
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  7. Atomic Layering Thermostable Antigen and Adjuvant (ALTAbioRxiv : the preprint server for biology · 2026
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11 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

10 authors.

Christopher O BarnesDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, 91125, USA.
Harry B GristickDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, 91125, USA.
Natalia T FreundLaboratory of Molecular Immunology, The Rockefeller University, New York, NY, 10065, USA.
Amelia EscolanoLaboratory of Molecular Immunology, The Rockefeller University, New York, NY, 10065, USA.
Artem Y LyubimovStanford Synchrotron Radiation Lightsource, 2575 Sand Hill Road, Menlo Park, CA, 94025, USA.
Harald HartwegerLaboratory of Molecular Immunology, The Rockefeller University, New York, NY, 10065, USA.
Anthony P WestDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, 91125, USA.
Aina E CohenStanford Synchrotron Radiation Lightsource, 2575 Sand Hill Road, Menlo Park, CA, 94025, USA.
Michel C NussenzweigLaboratory of Molecular Immunology, The Rockefeller University, New York, NY, 10065, USA.
Pamela J BjorkmanDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, 91125, USA. bjorkman@caltech.edu.

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
Stuctural basis of bNab activityP01AI100148 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Pamela J Bjorkman · 2013 to 2026
$43.3M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
NIAID NIH HHS P01 AI100148NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P50 GM082545
6 · The paper itself

Abstract

Broadly neutralizing antibodies (bNAbs) isolated from HIV-1-infected individuals inform HIV-1 vaccine design efforts. Developing bNAbs with increased efficacy requires understanding how antibodies interact with the native oligomannose and complex-type N-glycan shield that hides most protein epitopes on HIV-1 envelope (Env). Here we present crystal structures, including a 3.8-Å X-ray free electron laser dataset, of natively glycosylated Env trimers complexed with BG18, the most potent V3/N332

Indexed as

AnimalsAntibodies, NeutralizingCHO CellsCricetinaeCricetulusCrystallography, X-Rayenv Gene Products, Human Immunodeficiency VirusEpitopesGlycosylationHEK293 CellsHIV-1HIV AntibodiesHIV Envelope Protein gp120HIV InfectionsHumansPolysaccharidesAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusEpitopesHIV AntibodiesHIV Envelope Protein gp120Polysaccharides

Identifiers

PMID29593217
PMCPMC5871869

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.