Evidence map›Paper›PMID 28548638›Full record

ArticleeLife2017

Asymmetric recognition of HIV-1 Envelope trimer by V1V2 loop-targeting antibodies.

Haoqing Wang, Harry B Gristick, Louise Scharf, Anthony P West, Rachel P Galimidi, Michael S Seaman, Natalia T Freund, Michel C Nussenzweig, Pamela J Bjorkman

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 60 citations in OpenAlex.

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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

9 authors at 3 institutions in 1 country.

Haoqing WangDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.ORCID 0000-0003-0277-3018
Harry B GristickDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Louise ScharfDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Anthony P WestDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Rachel P GalimidiDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Michael S SeamanBeth Israel Deaconess Medical Center, Boston, United States.
Natalia T FreundLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.
Michel C NussenzweigLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.
Pamela J BjorkmanDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.ORCID 0000-0002-2277-3990
California Institute of Technology · USRockefeller University · USBeth Israel Deaconess Medical Center · US

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI HOPE, THOMAS · 2007 to 2018
$51.1M
Stuctural basis of bNab activityP01AI100148 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Pamela J Bjorkman · 2013 to 2026
$43.3M
Molecular Electron Microscopy Core Facility ImprovementsG20RR031199 · NCRR · UNIVERSITY OF VIRGINIA · PI SHUPNIK, MARGARET A · 2010 to 2010
$2.0M
300 keV Liquid Helium Robotic MicroscopeS10RR025067 · NCRR · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2009 to 2009
$2.0M
Direct Electron Detector for a Titan Krios Robotic Electron Cryo-MicroscopeS10OD018149 · OD · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H., YEAGER, MARK JAY · 2014 to 2014
$500k
NCRR NIH HHS G20 RR031199NCRR NIH HHS S10 RR025067NIAID NIH HHS P01 AI100148NIGMS NIH HHS P50 GM082545NIH HHS S10 OD018149
6 · The paper itself

Abstract

The HIV-1 envelope (Env) glycoprotein binds to host cell receptors to mediate membrane fusion. The prefusion Env trimer is stabilized by V1V2 loops that interact at the trimer apex. Broadly neutralizing antibodies (bNAbs) against V1V2 loops, exemplified by PG9, bind asymmetrically as a single Fab to the apex of the symmetric Env trimer using a protruding CDRH3 to penetrate the Env glycan shield. Here we characterized a distinct mode of V1V2 epitope recognition by the new bNAb BG1 in which two Fabs bind asymmetrically per Env trimer using a compact CDRH3. Comparisons between cryo-EM structures of Env trimer complexed with BG1 (6.2 Å resolution) and PG9 (11.5 Å resolution) revealed a new V1V2-targeting strategy by BG1. Analyses of the EM structures provided information relevant to vaccine design including molecular details for different modes of asymmetric recognition of Env trimer and a binding model for BG1 recognition of V1V2 involving glycan flexibility.

Indexed as

Antibodies, NeutralizingCryoelectron Microscopyenv Gene Products, Human Immunodeficiency VirusHIV AntibodiesHumansImmunoglobulin Fab FragmentsProtein BindingAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusHIV AntibodiesImmunoglobulin Fab Fragmentsbiophysicsbroadly neutralizing antibodiesCryo-EMHumanstructural biologyvirus

Identifiers

PMID28548638
PMCPMC5472438
OpenAlexW2617901758

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.